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><channel><title>Natural Sciences Bibliography &#187; Purification</title> <atom:link href="http://scien.net/category/chromatography/purification/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>160,000 References and 120,000 Tags</description> <lastBuildDate>Sat, 11 May 2013 06:06:13 +0000</lastBuildDate> <language>en-US</language> <sy:updatePeriod>hourly</sy:updatePeriod> <sy:updateFrequency>1</sy:updateFrequency> <generator>http://wordpress.org/?v=3.5.1</generator> <item><title>Staphylococcus hyicus-skin reactions in piglets caused by crude extracellular products and by partially purified exfoliative toxin</title><link>http://scien.net/chromatography/purification/staphylococcus-hyicus-skin-reactions-in-piglets-caused-by-crude-extracellular-products-and-by-partially-purified-exfoliative-toxin</link> <comments>http://scien.net/chromatography/purification/staphylococcus-hyicus-skin-reactions-in-piglets-caused-by-crude-extracellular-products-and-by-partially-purified-exfoliative-toxin#comments</comments> <pubDate>Sat, 11 May 2013 05:50:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[acanthosis]]></category> <category><![CDATA[epidermitis]]></category> <category><![CDATA[exfoliation]]></category> <category><![CDATA[exfoliative]]></category> <category><![CDATA[hyicus]]></category> <category><![CDATA[macroscopical]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/staphylococcus-hyicus-skin-reactions-in-piglets-caused-by-crude-extracellular-products-and-by-partially-purified-exfoliative-toxin</guid> <description><![CDATA[Andersen, Lars Ole; Wegener, Henrik Caspar; Bille Hansen, Vivi, 1993: Staphylococcus hyicus-skin reactions in piglets caused by crude extracellular products and by partially purified exfoliative toxin. Microbial Pathogenesis. 15(3): 217-225 Staphylococcus hyicus may cause a spontaneous generalized exudative epidermitis in piglets. The progression and regression of macroscopical and histopathological lesions in piglet skin after subcutaneous [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/staphylococcus-hyicus-skin-reactions-in-piglets-caused-by-crude-extracellular-products-and-by-partially-purified-exfoliative-toxin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Specific and abundant secretion of a novel hydroxyproline-rich glycoprotein from salt-adapted winged bean cells</title><link>http://scien.net/chromatography/purification/specific-and-abundant-secretion-of-a-novel-hydroxyproline-rich-glycoprotein-from-salt-adapted-winged-bean-cells</link> <comments>http://scien.net/chromatography/purification/specific-and-abundant-secretion-of-a-novel-hydroxyproline-rich-glycoprotein-from-salt-adapted-winged-bean-cells#comments</comments> <pubDate>Sat, 11 May 2013 05:43:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[tetrahydroxyproline]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/specific-and-abundant-secretion-of-a-novel-hydroxyproline-rich-glycoprotein-from-salt-adapted-winged-bean-cells</guid> <description><![CDATA[Esaka, M; Hayakawa, H; Hashimoto, M; Matsubara, N., 1992: Specific and abundant secretion of a novel hydroxyproline-rich glycoprotein from salt-adapted winged bean cells. Plant physiology 100(3): 1339-1345 Winged bean callus was adapted to increasing concentrations of NaCl by sequential transfer to medium with 0, 0.5, 1.0, 1.5, and 2.0% (w/v) NaCl. When the culture media, [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/specific-and-abundant-secretion-of-a-novel-hydroxyproline-rich-glycoprotein-from-salt-adapted-winged-bean-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Role of pseudorabies virus glycoprotein II in protection from lethal infection</title><link>http://scien.net/chromatography/purification/role-of-pseudorabies-virus-glycoprotein-ii-in-protection-from-lethal-infection</link> <comments>http://scien.net/chromatography/purification/role-of-pseudorabies-virus-glycoprotein-ii-in-protection-from-lethal-infection#comments</comments> <pubDate>Sat, 11 May 2013 04:57:45 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[nonidet]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/role-of-pseudorabies-virus-glycoprotein-ii-in-protection-from-lethal-infection</guid> <description><![CDATA[Nakamura, Toshihiro; Ihara, Takeshi; Nunoya, Tetsuo; Kuwahara, Hiroyoshi; Ishihama, Akira; Ueda, Susumu, 1993: Role of pseudorabies virus glycoprotein II in protection from lethal infection. Veterinary Microbiology. 36(1-2): 83-90 A monoclonal antibody (mAb), named 1.21, with complement-dependent neutralizing activity was produced against glycoprotein Ii (gII) of pseudorabies virus (Prv). By immunoaffinity chromatography using a mAB 1.21 [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/role-of-pseudorabies-virus-glycoprotein-ii-in-protection-from-lethal-infection/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Relation between proteolysis and astringent off-flavor in milk</title><link>http://scien.net/chromatography/purification/relation-between-proteolysis-and-astringent-off-flavor-in-milk</link> <comments>http://scien.net/chromatography/purification/relation-between-proteolysis-and-astringent-off-flavor-in-milk#comments</comments> <pubDate>Sat, 11 May 2013 03:55:16 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[astringencies]]></category> <category><![CDATA[astringency]]></category> <category><![CDATA[micromoleml]]></category> <category><![CDATA[nonspecifically]]></category> <category><![CDATA[organoleptically]]></category> <category><![CDATA[psychrotroph]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/relation-between-proteolysis-and-astringent-off-flavor-in-milk</guid> <description><![CDATA[Harwalkar, Vr; Cholette, H; Mckellar, Rc; Emmons, Db, 1993: Relation between proteolysis and astringent off-flavor in milk. Journal of dairy science 76(9): 2521-2527 Pasteurized skim milk was treated with 10 proteinases from psychrotrophic bacteria and with plasmin, the naturally occurring milk proteinase, and evaluated organoleptically for astringency. At comparable levels of digestion (extent of proteolysis [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/relation-between-proteolysis-and-astringent-off-flavor-in-milk/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Reconstitution and characterization of a calmodulin-stimulated Ca2+-pumping ATPase purified from Brassica oleracea L</title><link>http://scien.net/chromatography/purification/reconstitution-and-characterization-of-a-calmodulin-stimulated-ca2-pumping-atpase-purified-from-brassica-oleracea-l</link> <comments>http://scien.net/chromatography/purification/reconstitution-and-characterization-of-a-calmodulin-stimulated-ca2-pumping-atpase-purified-from-brassica-oleracea-l#comments</comments> <pubDate>Sat, 11 May 2013 03:47:35 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/reconstitution-and-characterization-of-a-calmodulin-stimulated-ca2-pumping-atpase-purified-from-brassica-oleracea-l</guid> <description><![CDATA[Askerlund, P; Evans, De, 1992: Reconstitution and characterization of a calmodulin-stimulated Ca2+-pumping ATPase purified from Brassica oleracea L. Plant physiology 100(4): 1670-1681 Purification and functional reconstitution of a calmodulin-stimulated Ca2+-ATPase from cauliflower (Brassica oleracea L.) is described. Activity was purified about 120-fold from a microsomal fraction using calmodulin-affinity chromatography. The purified fraction showed a polypeptide [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/reconstitution-and-characterization-of-a-calmodulin-stimulated-ca2-pumping-atpase-purified-from-brassica-oleracea-l/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Rapid degradation of cucumber cotyledon lipoxygenase</title><link>http://scien.net/chromatography/purification/rapid-degradation-of-cucumber-cotyledon-lipoxygenase</link> <comments>http://scien.net/chromatography/purification/rapid-degradation-of-cucumber-cotyledon-lipoxygenase#comments</comments> <pubDate>Sat, 11 May 2013 03:42:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[deembryonated]]></category> <category><![CDATA[lipoxygenases]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/rapid-degradation-of-cucumber-cotyledon-lipoxygenase</guid> <description><![CDATA[Matsui, Kenji; Irie, Makoto; Kajiwara, Tadahiko; Kakuno, Tomisaburo; Hatanaka, Akikazu, 1993: Rapid degradation of cucumber cotyledon lipoxygenase. Phytochemistry (oxford). 32(6): 1387-1391 The lipoxygenase activity from cucumber cotyledons grown with their embryonic axis was separated into two fractions having M-rs of 90,000 and 96,000, respectively, by hydrophobic chromatography. However, from deembryonated cucumber cotyledons, only one form [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/rapid-degradation-of-cucumber-cotyledon-lipoxygenase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification, characterization, and complete amino acid sequence of a trypsin inhibitor from amaranth (Amaranthus hypochondriacus) seeds</title><link>http://scien.net/chromatography/purification/purification-characterization-and-complete-amino-acid-sequence-of-a-trypsin-inhibitor-from-amaranth-amaranthus-hypochondriacus-seeds</link> <comments>http://scien.net/chromatography/purification/purification-characterization-and-complete-amino-acid-sequence-of-a-trypsin-inhibitor-from-amaranth-amaranthus-hypochondriacus-seeds#comments</comments> <pubDate>Sat, 11 May 2013 03:34:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[hypochondriacus]]></category> <category><![CDATA[peruvianum]]></category> <category><![CDATA[prostephanus]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-characterization-and-complete-amino-acid-sequence-of-a-trypsin-inhibitor-from-amaranth-amaranthus-hypochondriacus-seeds</guid> <description><![CDATA[Valdes Rodriguez, S.; Segura Nieto, M.; Chagolla Lopez, A.; Verver y Vargas Cortina, A.; Martinez Gallardo, N.; Blanco Labra, A., 1993: Purification, characterization, and complete amino acid sequence of a trypsin inhibitor from amaranth (Amaranthus hypochondriacus) seeds. Plant Physiology 103(4): 1407-1412 A protein proteinase inhibitor was purified from a seed extract of amaranth (Amaranthus hypochondriacus) [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-characterization-and-complete-amino-acid-sequence-of-a-trypsin-inhibitor-from-amaranth-amaranthus-hypochondriacus-seeds/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of recombinant budgerigar fledgling disease virus VP1 capsid protein and its ability for in vitro capsid assembly</title><link>http://scien.net/chromatography/purification/purification-of-recombinant-budgerigar-fledgling-disease-virus-vp1-capsid-protein-and-its-ability-for-in-vitro-capsid-assembly</link> <comments>http://scien.net/chromatography/purification/purification-of-recombinant-budgerigar-fledgling-disease-virus-vp1-capsid-protein-and-its-ability-for-in-vitro-capsid-assembly#comments</comments> <pubDate>Sat, 11 May 2013 03:34:07 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[capsomeres]]></category> <category><![CDATA[pentameric]]></category> <category><![CDATA[pflag]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-recombinant-budgerigar-fledgling-disease-virus-vp1-capsid-protein-and-its-ability-for-in-vitro-capsid-assembly</guid> <description><![CDATA[Rodgers, Red; Chang, D; Cai, X; Consigli, Ra, 1994: Purification of recombinant budgerigar fledgling disease virus VP1 capsid protein and its ability for in vitro capsid assembly. Journal of virology 68(5): 3386-3390 A recombinant system for the major capsid Vp1 protein of budgerigar fledgling disease virus has been established. The Vp1 gene was inserted into [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-recombinant-budgerigar-fledgling-disease-virus-vp1-capsid-protein-and-its-ability-for-in-vitro-capsid-assembly/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of hemagglutinin from Haemophilus paragallinarum using monoclonal antibody</title><link>http://scien.net/chromatography/purification/purification-of-hemagglutinin-from-haemophilus-paragallinarum-using-monoclonal-antibody</link> <comments>http://scien.net/chromatography/purification/purification-of-hemagglutinin-from-haemophilus-paragallinarum-using-monoclonal-antibody#comments</comments> <pubDate>Sat, 11 May 2013 03:34:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[paragallinarum]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-hemagglutinin-from-haemophilus-paragallinarum-using-monoclonal-antibody</guid> <description><![CDATA[Takagi, Masami; Hirayama, Norio; Simazaki, Tomoaki; Taguchi, Kunihiko; Yamaoka, Ryouzou; Ohta, Shuichi, 1993: Purification of hemagglutinin from Haemophilus paragallinarum using monoclonal antibody. Veterinary Microbiology. 34(2): 197 The purification of hemagglutinin from Haemophilus paragallinarum was attempted using affinity chromatography with monoclonal antibody. The antigen eluted from the affinity column using potassium thiocyanate buffer agglutinated chicken erythrocytes. [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-hemagglutinin-from-haemophilus-paragallinarum-using-monoclonal-antibody/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of extensin from cell walls of tomato (hybrid of Lycopersicon esculentum and L. peruvianum) cells in suspension culture</title><link>http://scien.net/chromatography/purification/purification-of-extensin-from-cell-walls-of-tomato-hybrid-of-lycopersicon-esculentum-and-l-peruvianum-cells-in-suspension-culture</link> <comments>http://scien.net/chromatography/purification/purification-of-extensin-from-cell-walls-of-tomato-hybrid-of-lycopersicon-esculentum-and-l-peruvianum-cells-in-suspension-culture#comments</comments> <pubDate>Sat, 11 May 2013 03:34:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[cluted]]></category> <category><![CDATA[extensin]]></category> <category><![CDATA[extensins]]></category> <category><![CDATA[insolubilized]]></category> <category><![CDATA[ionically]]></category> <category><![CDATA[peruvianum]]></category> <category><![CDATA[superose]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-extensin-from-cell-walls-of-tomato-hybrid-of-lycopersicon-esculentum-and-l-peruvianum-cells-in-suspension-culture</guid> <description><![CDATA[Brownleader, M. D.; Dey, P. M., 1993: Purification of extensin from cell walls of tomato (hybrid of Lycopersicon esculentum and L. peruvianum) cells in suspension culture. Planta 191(4): 457-469 Extensin, a hydroxyproline-rich glycoprotein comprising substantial amounts of beta-L-arabinose-hydroxyproline glycosidic linkages is believed to be insolubilized in the cell wall during host-pathogen interaction by a peroxidase/hydroperoxide-mediated [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-extensin-from-cell-walls-of-tomato-hybrid-of-lycopersicon-esculentum-and-l-peruvianum-cells-in-suspension-culture/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of antibacterial proteins in Heliothis assulta injected with Bacillus thuringiensis</title><link>http://scien.net/chromatography/purification/purification-of-antibacterial-proteins-in-heliothis-assulta-injected-with-bacillus-thuringiensis</link> <comments>http://scien.net/chromatography/purification/purification-of-antibacterial-proteins-in-heliothis-assulta-injected-with-bacillus-thuringiensis#comments</comments> <pubDate>Sat, 11 May 2013 03:33:59 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[assulta]]></category> <category><![CDATA[haemocoel]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-antibacterial-proteins-in-heliothis-assulta-injected-with-bacillus-thuringiensis</guid> <description><![CDATA[Myung, Yoo Chong; Jeong, Seong Eun; Lee, Hyung Chul, 1994: Purification of antibacterial proteins in Heliothis assulta injected with Bacillus thuringiensis. Korean Journal Of Zoology. 37(2): 274-280 To investigate characteristics of antibacterial proteins in haemolymph of Heliothis assulta, Bacillus thuringiensis were injected into haemocoel of the mature larvae. The highest antibacterial activity was induced at [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-antibacterial-proteins-in-heliothis-assulta-injected-with-bacillus-thuringiensis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of an infection-related, extracellular peroxidase from barley</title><link>http://scien.net/chromatography/purification/purification-of-an-infection-related-extracellular-peroxidase-from-barley</link> <comments>http://scien.net/chromatography/purification/purification-of-an-infection-related-extracellular-peroxidase-from-barley#comments</comments> <pubDate>Sat, 11 May 2013 03:33:58 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[marchal]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-an-infection-related-extracellular-peroxidase-from-barley</guid> <description><![CDATA[Kerby, K; Somerville, Sc, 1992: Purification of an infection-related, extracellular peroxidase from barley. Plant physiology 100(1): 397-402 Increases in two extracellular peroxidases were observed following inoculation of barley (Hordeum vulgare L.) with the powdery mildew pathogen Erysiphe graminis Dc.: Fr. f. sp. hordei Em. Marchal). The more prominent isozyme, P8.5, was purified from intercellular wash [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-an-infection-related-extracellular-peroxidase-from-barley/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of a tonoplast polypeptide with sucrose transport properties</title><link>http://scien.net/chromatography/purification/purification-of-a-tonoplast-polypeptide-with-sucrose-transport-properties</link> <comments>http://scien.net/chromatography/purification/purification-of-a-tonoplast-polypeptide-with-sucrose-transport-properties#comments</comments> <pubDate>Sat, 11 May 2013 03:33:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[proteoliposomes]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-a-tonoplast-polypeptide-with-sucrose-transport-properties</guid> <description><![CDATA[Thom, Margaret; Getz, Hans Peter; Maretzki, Andrew, 1992: Purification of a tonoplast polypeptide with sucrose transport properties. Physiologia Plantarum. 86(1): 104-114 Sucrose uptake into vacuoles of sugarcane parenchyma cells is mediated by a transporter. A polypeptide fitting that description has been partially purified from solubilized tonoplast by gel filtration and ion exchange chromatography. Purification of [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-a-tonoplast-polypeptide-with-sucrose-transport-properties/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of a copper binding peptide from the mushroom Grifola frondosa and its effect on copper absorption</title><link>http://scien.net/chromatography/purification/purification-of-a-copper-binding-peptide-from-the-mushroom-grifola-frondosa-and-its-effect-on-copper-absorption</link> <comments>http://scien.net/chromatography/purification/purification-of-a-copper-binding-peptide-from-the-mushroom-grifola-frondosa-and-its-effect-on-copper-absorption#comments</comments> <pubDate>Sat, 11 May 2013 03:33:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[frondosa]]></category> <category><![CDATA[grifola]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-a-copper-binding-peptide-from-the-mushroom-grifola-frondosa-and-its-effect-on-copper-absorption</guid> <description><![CDATA[Shimaoka, Iwao; Kodama, Junko; Nishino, Kohsuke; Itokawa, Yoshinori, 1993: Purification of a copper binding peptide from the mushroom Grifola frondosa and its effect on copper absorption. Journal Of Nutritional Biochemistry. 4(1): 33-38 The present studies were undertaken to investigate the effect of a copper binding peptide on copper bioavailability. This peptide was extracted from the [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-a-copper-binding-peptide-from-the-mushroom-grifola-frondosa-and-its-effect-on-copper-absorption/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of a 74-kilodalton surface glycoprotein from heart myoblasts that inhibits binding and entry of Trypanosoma cruzi into heart cells</title><link>http://scien.net/chromatography/purification/purification-of-a-74-kilodalton-surface-glycoprotein-from-heart-myoblasts-that-inhibits-binding-and-entry-of-trypanosoma-cruzi-into-heart-cells</link> <comments>http://scien.net/chromatography/purification/purification-of-a-74-kilodalton-surface-glycoprotein-from-heart-myoblasts-that-inhibits-binding-and-entry-of-trypanosoma-cruzi-into-heart-cells#comments</comments> <pubDate>Sat, 11 May 2013 03:33:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[isoelectrofocusing]]></category> <category><![CDATA[trypomastigote]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-of-a-74-kilodalton-surface-glycoprotein-from-heart-myoblasts-that-inhibits-binding-and-entry-of-trypanosoma-cruzi-into-heart-cells</guid> <description><![CDATA[Villalta, Fernando; Ruiz Ruano, Antonio; Valentine, Anthony A.; Lima, Maria F., 1993: Purification of a 74-kilodalton surface glycoprotein from heart myoblasts that inhibits binding and entry of Trypanosoma cruzi into heart cells. Molecular &#038; Biochemical Parasitology. 61(2): 217-230 We have identified and purified a 74 kDa surface glycoprotein from heart myoblasts that specifically binds to [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-of-a-74-kilodalton-surface-glycoprotein-from-heart-myoblasts-that-inhibits-binding-and-entry-of-trypanosoma-cruzi-into-heart-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and properties of the fatty acid-binding VHDL from the hemolymph of the spider Eurypelma californicum</title><link>http://scien.net/chromatography/purification/purification-and-properties-of-the-fatty-acid-binding-vhdl-from-the-hemolymph-of-the-spider-eurypelma-californicum</link> <comments>http://scien.net/chromatography/purification/purification-and-properties-of-the-fatty-acid-binding-vhdl-from-the-hemolymph-of-the-spider-eurypelma-californicum#comments</comments> <pubDate>Sat, 11 May 2013 03:33:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[californicum]]></category> <category><![CDATA[eurypelma]]></category> <category><![CDATA[tarantula]]></category> <category><![CDATA[vhdl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-properties-of-the-fatty-acid-binding-vhdl-from-the-hemolymph-of-the-spider-eurypelma-californicum</guid> <description><![CDATA[Stratakis, Emmanoel; Fragkiadakis, Georgios; Tentes, Ioannis, 1993: Purification and properties of the fatty acid-binding VHDL from the hemolymph of the spider Eurypelma californicum. Journal Of Experimental Zoology. 267(5): 483-492 An abundant, very high density lipoprotein (Vhdl) was isolated from the hemolymph of male and female tarantula Eurypelma californicum. The purification procedure involved density gradient ultracentrifugation [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-properties-of-the-fatty-acid-binding-vhdl-from-the-hemolymph-of-the-spider-eurypelma-californicum/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and partial characterization of trypsin/chymotrypsin inhibitors from cabbage foliage</title><link>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-trypsinchymotrypsin-inhibitors-from-cabbage-foliage</link> <comments>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-trypsinchymotrypsin-inhibitors-from-cabbage-foliage#comments</comments> <pubDate>Sat, 11 May 2013 03:33:39 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[trypsinchymotrypsin]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-partial-characterization-of-trypsinchymotrypsin-inhibitors-from-cabbage-foliage</guid> <description><![CDATA[Broadway, Roxanne M., 1993: Purification and partial characterization of trypsin/chymotrypsin inhibitors from cabbage foliage. Phytochemistry (oxford). 33(1): 21-27 Proteinase inhibitors from cabbage foliage (Brassica oleracea) had trypsin and chymotrypsin inhibitory activity that was relatively stable over a broad range of temperatures (0-100 degree) and pH values (4.5-7.5). The six proteinase inhibitors that were purified by [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-trypsinchymotrypsin-inhibitors-from-cabbage-foliage/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and partial characterization of a host-specific pathotoxin from culture filtrates of Septoria glycines</title><link>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-a-host-specific-pathotoxin-from-culture-filtrates-of-septoria-glycines</link> <comments>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-a-host-specific-pathotoxin-from-culture-filtrates-of-septoria-glycines#comments</comments> <pubDate>Sat, 11 May 2013 03:33:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[carbazole]]></category> <category><![CDATA[pathotoxin]]></category> <category><![CDATA[vacuo]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-partial-characterization-of-a-host-specific-pathotoxin-from-culture-filtrates-of-septoria-glycines</guid> <description><![CDATA[Song, H. S.; Lim, S. M.; Clark, J. M.Jr, 1993: Purification and partial characterization of a host-specific pathotoxin from culture filtrates of Septoria glycines. Phytopathology. 83(6): 659-661 A host-specific pathotoxin isolated from culture filtrate of Septoria glycines caused typical symptoms of brown spot disease on cotyledons and leaves of soybean (Glycine max). This toxin was [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-partial-characterization-of-a-host-specific-pathotoxin-from-culture-filtrates-of-septoria-glycines/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and molecular cloning of bovine oviduct-specific glycoprotein</title><link>http://scien.net/chromatography/purification/purification-and-molecular-cloning-of-bovine-oviduct-specific-glycoprotein</link> <comments>http://scien.net/chromatography/purification/purification-and-molecular-cloning-of-bovine-oviduct-specific-glycoprotein#comments</comments> <pubDate>Sat, 11 May 2013 03:33:35 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[bogp]]></category> <category><![CDATA[microsequencing]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-molecular-cloning-of-bovine-oviduct-specific-glycoprotein</guid> <description><![CDATA[Sendai, Y; Abe, H; Kikuchi, M; Satoh, T; Hoshi, H., 1994: Purification and molecular cloning of bovine oviduct-specific glycoprotein. Biology of reproduction 50(4): 927-934 A specific 85-97-kDa (95-kDa) glycoprotein was found in bovine oviductal tissue and fluid during the follicular phase. In this study, a 95-kDa bovine oviductal glycoprotein (95-kDa Bogp) was purified by wheat [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-molecular-cloning-of-bovine-oviduct-specific-glycoprotein/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea</title><link>http://scien.net/chromatography/purification/purification-and-initial-characterization-of-the-proteasome-from-the-higher-plant-spinacia-oleracea</link> <comments>http://scien.net/chromatography/purification/purification-and-initial-characterization-of-the-proteasome-from-the-higher-plant-spinacia-oleracea#comments</comments> <pubDate>Sat, 11 May 2013 03:33:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[multicatalytic]]></category> <category><![CDATA[proteasomes]]></category> <category><![CDATA[toyopearl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-initial-characterization-of-the-proteasome-from-the-higher-plant-spinacia-oleracea</guid> <description><![CDATA[Ozaki, M; Fujinami, K; Tanaka, K; Amemiya, Y; Sato, T; Ogura, N; Nakagawa, H., 1992: Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea. Journal of biological chemistry, 267(30): 21678-21684 The proteasome (multicatalytic protease complex), a high molecular weight protein complex, has been purified from spinach leaves by successive chromatography on [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-initial-characterization-of-the-proteasome-from-the-higher-plant-spinacia-oleracea/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of prophenoloxidases from pupae of Drosophila melanogaster</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-prophenoloxidases-from-pupae-of-drosophila-melanogaster</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-prophenoloxidases-from-pupae-of-drosophila-melanogaster#comments</comments> <pubDate>Sat, 11 May 2013 03:33:19 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[prophenoloxidase]]></category> <category><![CDATA[prophenoloxidases]]></category> <category><![CDATA[sepharcyl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-prophenoloxidases-from-pupae-of-drosophila-melanogaster</guid> <description><![CDATA[Fujimoto, Kengo; Masuda, Ken Ichiro; Asada, Nobuhiko; Ohnishi, Eiji, 1993: Purification and characterization of prophenoloxidases from pupae of Drosophila melanogaster. Journal Of Biochemistry (tokyo). 113(3): 285-291 Two isoforms of prophenoloxidase were isolated from pupae of Oregon-R strain of Drosophila melanogaster. The purification procedure included ammonium sulfate fractionation, Sepharcyl S-200 gel chromatography, Deae-cellulose, and hydroxylapatite column [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-prophenoloxidases-from-pupae-of-drosophila-melanogaster/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of glutathione reductase isozymes specific for the state of cold hardiness of red spruce</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-glutathione-reductase-isozymes-specific-for-the-state-of-cold-hardiness-of-red-spruce</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-glutathione-reductase-isozymes-specific-for-the-state-of-cold-hardiness-of-red-spruce#comments</comments> <pubDate>Sat, 11 May 2013 03:33:12 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[acclimination]]></category> <category><![CDATA[nonhardened]]></category> <category><![CDATA[sarg]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-glutathione-reductase-isozymes-specific-for-the-state-of-cold-hardiness-of-red-spruce</guid> <description><![CDATA[Hausladen, A; Alscher, Rg, 1994: Purification and characterization of glutathione reductase isozymes specific for the state of cold hardiness of red spruce. Plant physiology 105(1): 205-213 Isozymes of glutathione reductase (Gr) have been purified from red spruce (Picea rubens Sarg.) needles. Two isozymes could be separated by anion-exchange chromatography from both nonhardened or cold-hardened tissue. [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-glutathione-reductase-isozymes-specific-for-the-state-of-cold-hardiness-of-red-spruce/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of cinnamyl alcohol dehydrogenase isoforms from the periderm of Eucalyptus gunnii Hook</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-cinnamyl-alcohol-dehydrogenase-isoforms-from-the-periderm-of-eucalyptus-gunnii-hook</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-cinnamyl-alcohol-dehydrogenase-isoforms-from-the-periderm-of-eucalyptus-gunnii-hook#comments</comments> <pubDate>Sat, 11 May 2013 03:33:07 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[adhs]]></category> <category><![CDATA[boudet]]></category> <category><![CDATA[cinnamyl]]></category> <category><![CDATA[coniferyl]]></category> <category><![CDATA[elute]]></category> <category><![CDATA[grima]]></category> <category><![CDATA[gunnii]]></category> <category><![CDATA[halpin]]></category> <category><![CDATA[hydroxycinnamyl]]></category> <category><![CDATA[joffroy]]></category> <category><![CDATA[monolignols]]></category> <category><![CDATA[pettenati]]></category> <category><![CDATA[schuch]]></category> <category><![CDATA[sinapyl]]></category> <category><![CDATA[suberin]]></category> <category><![CDATA[suberized]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-cinnamyl-alcohol-dehydrogenase-isoforms-from-the-periderm-of-eucalyptus-gunnii-hook</guid> <description><![CDATA[Hawkins, Sw; Boudet, Am, 1994: Purification and characterization of cinnamyl alcohol dehydrogenase isoforms from the periderm of Eucalyptus gunnii Hook. Plant physiology 104(1): 75-84 Cinnamyl alcohol dehydrogenase (Cad, Ec 1.1.1.195) isoforms were purified from the periderm (containing both suberized and lignified cell layers) of Eucalyptus gunnii Hook stems. Two isoforms (Cad 1p and Cad 2p) [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-cinnamyl-alcohol-dehydrogenase-isoforms-from-the-periderm-of-eucalyptus-gunnii-hook/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of carboxylesterases of a rice brown planthopper, Nilaparvata lugens Stal</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-carboxylesterases-of-a-rice-brown-planthopper-nilaparvata-lugens-stal</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-carboxylesterases-of-a-rice-brown-planthopper-nilaparvata-lugens-stal#comments</comments> <pubDate>Sat, 11 May 2013 03:33:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[carboxylesterases]]></category> <category><![CDATA[cincticeps]]></category> <category><![CDATA[furcifera]]></category> <category><![CDATA[laodelphax]]></category> <category><![CDATA[malaoxon]]></category> <category><![CDATA[nephotettix]]></category> <category><![CDATA[oxons]]></category> <category><![CDATA[planthoppers]]></category> <category><![CDATA[sogatella]]></category> <category><![CDATA[striatellus]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-carboxylesterases-of-a-rice-brown-planthopper-nilaparvata-lugens-stal</guid> <description><![CDATA[Chen, Wen Lin; Sun, Chih Ning, 1994: Purification and characterization of carboxylesterases of a rice brown planthopper, Nilaparvata lugens Stal. Insect Biochemistry &#038; Molecular Biology. 24(4): 347-355 More than 10 molecular forms of carboxylesterases were observed with alpha-naphthyl acetate as substrate in a rice brown planthopper (Bph), Nilaparvata lugens Stal, using isoelectric focusing. The three [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-carboxylesterases-of-a-rice-brown-planthopper-nilaparvata-lugens-stal/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of an agglutinin from the hemolymph of Locusta migratoria (Orthoptera)</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-an-agglutinin-from-the-hemolymph-of-locusta-migratoria-orthoptera</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-an-agglutinin-from-the-hemolymph-of-locusta-migratoria-orthoptera#comments</comments> <pubDate>Sat, 11 May 2013 03:33:01 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[ferguson]]></category> <category><![CDATA[rrbc]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-an-agglutinin-from-the-hemolymph-of-locusta-migratoria-orthoptera</guid> <description><![CDATA[Drif, L.; Brehelin, M., 1994: Purification and characterization of an agglutinin from the hemolymph of Locusta migratoria (Orthoptera). Insect Biochemistry and Molecular Biology 24(3): 283-289 An agglutinin from plasma of the locust Locusta migratoria was purified to apparent homogeneity by one step affinity chromatography. Two kinds of affinity columns were used which gave the same [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-an-agglutinin-from-the-hemolymph-of-locusta-migratoria-orthoptera/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of an N-acetyllactosamine-specific lectin from larvae of a moth, Phalera flavescens</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-larvae-of-a-moth-phalera-flavescens</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-larvae-of-a-moth-phalera-flavescens#comments</comments> <pubDate>Sat, 11 May 2013 03:33:01 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[acetyllactosamine]]></category> <category><![CDATA[cellulofine]]></category> <category><![CDATA[desialylated]]></category> <category><![CDATA[heterotetrameric]]></category> <category><![CDATA[nonsubstituted]]></category> <category><![CDATA[phalera]]></category> <category><![CDATA[synsorbs]]></category> <category><![CDATA[toyopearl]]></category> <category><![CDATA[unglycosylated]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-larvae-of-a-moth-phalera-flavescens</guid> <description><![CDATA[Umetsu, Kazuo; Yamashita, Katsuko; Suzuki, Jun Ichi; Yamashita, Takao; Suzuki, Tsuneo, 1993: Purification and characterization of an N-acetyllactosamine-specific lectin from larvae of a moth, Phalera flavescens. Archives Of Biochemistry &#038; Biophysics. 301(1): 200-205 A lectin (Phalera flavescens agglutinin, Pfa) of a moth (P. flavescens) has been isolated from hemolymph by Deae-Toyopearl followed by Cellulofine Gcl-1000 [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-larvae-of-a-moth-phalera-flavescens/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-aconitase-isoforms-from-etiolated-pumpkin-cotyledons</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-aconitase-isoforms-from-etiolated-pumpkin-cotyledons#comments</comments> <pubDate>Sat, 11 May 2013 03:33:00 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[aconitase]]></category> <category><![CDATA[glyoxysomal]]></category> <category><![CDATA[glyoxysomes]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-aconitase-isoforms-from-etiolated-pumpkin-cotyledons</guid> <description><![CDATA[De Bellis, Luigi; Tsugeki, Ryuji; Alpi, Amedeo; Nishimura, Mikio, 1993: Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons. Physiologia Plantarum. 88(3): 485-492 Although aconitase (Ec 4.2.1.3) is involved in the glyoxylate cycle, which is localized in glyoxysomes, we detected very low aconitase activity in glyoxysomal fractions after sucrose gradient centrifugation of extracts prepared [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-aconitase-isoforms-from-etiolated-pumpkin-cotyledons/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a galactose-specific lectin from Psilocybe barrerae</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-a-galactose-specific-lectin-from-psilocybe-barrerae</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-a-galactose-specific-lectin-from-psilocybe-barrerae#comments</comments> <pubDate>Sat, 11 May 2013 03:32:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[barrerae]]></category> <category><![CDATA[psilocybe]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-a-galactose-specific-lectin-from-psilocybe-barrerae</guid> <description><![CDATA[Hernandez, E; Ortiz, R; Lopez, F; Masso, F; Montano, Lf; Martinage, A; Zenteno, E., 1993: Purification and characterization of a galactose-specific lectin from Psilocybe barrerae. Phytochemistry 32(5): 1209-1211 A Mr 28,000 galactose-specific lectin from the mushroom Psilocybe barrerae has been isolated and purified by single step affinity chromatography on a horse red blood cell stroma [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-a-galactose-specific-lectin-from-psilocybe-barrerae/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a fungal protease specific protein inhibitor (FPI-F) in the silkworm haemolymph</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-a-fungal-protease-specific-protein-inhibitor-fpi-f-in-the-silkworm-haemolymph</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-a-fungal-protease-specific-protein-inhibitor-fpi-f-in-the-silkworm-haemolymph#comments</comments> <pubDate>Sat, 11 May 2013 03:32:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[toyopearl]]></category> <category><![CDATA[uncompetitively]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-a-fungal-protease-specific-protein-inhibitor-fpi-f-in-the-silkworm-haemolymph</guid> <description><![CDATA[Eguchi, M.; Itoh, M.; Chou, L. Y.; Nishino, K., 1993: Purification and characterization of a fungal protease specific protein inhibitor (FPI-F) in the silkworm haemolymph. Comparative Biochemistry and Physiology B, Comparative Biochemistry 104(3): 537-543 One of fungal protease inhibitors (Fpi-F) in the haemolymph of the silkworm, Bombyx mori, was purified by ammonium sulphate precipitation, acid [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-a-fungal-protease-specific-protein-inhibitor-fpi-f-in-the-silkworm-haemolymph/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a flavin-binding storage protein from the hemolymph of Galleria mellonella</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-a-flavin-binding-storage-protein-from-the-hemolymph-of-galleria-mellonella</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-a-flavin-binding-storage-protein-from-the-hemolymph-of-galleria-mellonella#comments</comments> <pubDate>Sat, 11 May 2013 03:32:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[affi]]></category> <category><![CDATA[molted]]></category> <category><![CDATA[uncharacteristically]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-a-flavin-binding-storage-protein-from-the-hemolymph-of-galleria-mellonella</guid> <description><![CDATA[Silhacek, Donald L.; Miller, Stephen G.; Murphy, Curtis L., 1994: Purification and characterization of a flavin-binding storage protein from the hemolymph of Galleria mellonella. Archives Of Insect Biochemistry &#038; Physiology. 25(1): 55-72 The 85k storage protein that accumulates in the hemolymph of Galleria melloneli during the final larval instar was isolated and purified from newly [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-a-flavin-binding-storage-protein-from-the-hemolymph-of-galleria-mellonella/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a cytochrome P-450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-a-cytochrome-p-450-from-insecticide-susceptible-and-resistant-strains-of-housefly-musca-domestica-l-before-and-after-phenobarbital-exposure</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-a-cytochrome-p-450-from-insecticide-susceptible-and-resistant-strains-of-housefly-musca-domestica-l-before-and-after-phenobarbital-exposure#comments</comments> <pubDate>Sat, 11 May 2013 03:32:43 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-a-cytochrome-p-450-from-insecticide-susceptible-and-resistant-strains-of-housefly-musca-domestica-l-before-and-after-phenobarbital-exposure</guid> <description><![CDATA[Scott, J. G.; Lee, S. S. T., 1993: Purification and characterization of a cytochrome P-450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure. Archives of Insect Biochemistry and Physiology 24(1): 1-19 A cytochrome P-450 (P-450) was purified from abdominal microsomes of untreated and phenobarbital treated susceptible (S+) [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-a-cytochrome-p-450-from-insecticide-susceptible-and-resistant-strains-of-housefly-musca-domestica-l-before-and-after-phenobarbital-exposure/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of Pisum seed trypsin inhibitors</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-pisum-seed-trypsin-inhibitors</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-pisum-seed-trypsin-inhibitors#comments</comments> <pubDate>Sat, 11 May 2013 03:32:40 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[birk]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-pisum-seed-trypsin-inhibitors</guid> <description><![CDATA[Domoney, C.; Welham, T.; Sidebottom, C., 1993: Purification and characterization of Pisum seed trypsin inhibitors. Journal Of Experimental Botany. 44(261): 701-709 Seed trypsin inhibitors have been purified from Pisum. Three groups of inhibitor were separated using column chromatography, whereas non-denaturing activity gels showed that five inhibitors could be distinguished. N-terminal sequence data obtained for two [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-pisum-seed-trypsin-inhibitors/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of Fus sI3596, a 65 kd allergen of Fusarium solani</title><link>http://scien.net/chromatography/purification/purification-and-characterization-of-fus-si3596-a-65-kd-allergen-of-fusarium-solani</link> <comments>http://scien.net/chromatography/purification/purification-and-characterization-of-fus-si3596-a-65-kd-allergen-of-fusarium-solani#comments</comments> <pubDate>Sat, 11 May 2013 03:32:40 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-characterization-of-fus-si3596-a-65-kd-allergen-of-fusarium-solani</guid> <description><![CDATA[Verma, J; Pasha, S; Gangal, Sv, 1994: Purification and characterization of Fus sI3596, a 65 kd allergen of Fusarium solani. Molecular and cellular biochemistry, 131(2): 157-166 A component of Fusarium solani (F. solani), identified as the major allergen, Fus s I3596* was purified to homogeneity from culture filtrate (Cf) by means of anion-exchange column chromatography, [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-characterization-of-fus-si3596-a-65-kd-allergen-of-fusarium-solani/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and biochemical properties of calmodulin in Entamoeba histolytica and its distribution during secretion of electron-dense granules</title><link>http://scien.net/chromatography/purification/purification-and-biochemical-properties-of-calmodulin-in-entamoeba-histolytica-and-its-distribution-during-secretion-of-electron-dense-granules</link> <comments>http://scien.net/chromatography/purification/purification-and-biochemical-properties-of-calmodulin-in-entamoeba-histolytica-and-its-distribution-during-secretion-of-electron-dense-granules#comments</comments> <pubDate>Sat, 11 May 2013 03:32:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[calmodulinmg]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/purification-and-biochemical-properties-of-calmodulin-in-entamoeba-histolytica-and-its-distribution-during-secretion-of-electron-dense-granules</guid> <description><![CDATA[Munoz, Maria De Lourdes; O&#8217;shea Alvarez, Maria Del Socorro; Perez Garcia, Javier; Weinbach, Eugene C.; Moreno, Miguel Angel; Torre, Margarita De La; Magos, Marco Antonio; Tovar, Rosalinda, 1992: Purification and biochemical properties of calmodulin in Entamoeba histolytica and its distribution during secretion of electron-dense granules. Comparative Biochemistry &#038; Physiology B Comparative Biochemistry. 103(3): 517-521 Calmodulin [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/purification-and-biochemical-properties-of-calmodulin-in-entamoeba-histolytica-and-its-distribution-during-secretion-of-electron-dense-granules/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Proteolytic processing of the mosquitocidal toxin from Bacillus sphaericus SSII-1</title><link>http://scien.net/chromatography/purification/proteolytic-processing-of-the-mosquitocidal-toxin-from-bacillus-sphaericus-ssii-1</link> <comments>http://scien.net/chromatography/purification/proteolytic-processing-of-the-mosquitocidal-toxin-from-bacillus-sphaericus-ssii-1#comments</comments> <pubDate>Sat, 11 May 2013 03:29:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[mosquitocidal]]></category> <category><![CDATA[ribosyltransferase]]></category> <category><![CDATA[ssii]]></category> <category><![CDATA[trysin]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/proteolytic-processing-of-the-mosquitocidal-toxin-from-bacillus-sphaericus-ssii-1</guid> <description><![CDATA[Thanabalu, T; Hindley, J; Berry, C., 1992: Proteolytic processing of the mosquitocidal toxin from Bacillus sphaericus SSII-1. Journal of bacteriology 174(15): 5051-5056 The 97-kDa protein Mtx21, derived from the 100-kDa mosquitocidal protein (Mtx) from Bacillus sphaericus Ssii-1 by the deletion of the putative signal sequence, was expressed as a fusion protein with glutathione S-transferase in [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/proteolytic-processing-of-the-mosquitocidal-toxin-from-bacillus-sphaericus-ssii-1/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains</title><link>http://scien.net/chromatography/purification/proteolysis-of-the-85-kilodalton-crystalline-cysteine-proteinase-inhibitor-from-potato-releases-functional-cystatin-domains</link> <comments>http://scien.net/chromatography/purification/proteolysis-of-the-85-kilodalton-crystalline-cysteine-proteinase-inhibitor-from-potato-releases-functional-cystatin-domains#comments</comments> <pubDate>Sat, 11 May 2013 03:29:39 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[carlsberg]]></category> <category><![CDATA[hoff]]></category> <category><![CDATA[multicystatin]]></category> <category><![CDATA[rodis]]></category> <category><![CDATA[stoichiometries]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/proteolysis-of-the-85-kilodalton-crystalline-cysteine-proteinase-inhibitor-from-potato-releases-functional-cystatin-domains</guid> <description><![CDATA[Walsh, Ta; Strickland, Ja, 1993: Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains. Plant physiology 103(4): 1227-1234 The protein crystals found in potato (Solanum tuberosum L.) tuber cells consist of a single 85-kD polypeptide. This polypeptide is an inhibitor of papain and other cysteine proteinases and is capable of [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/proteolysis-of-the-85-kilodalton-crystalline-cysteine-proteinase-inhibitor-from-potato-releases-functional-cystatin-domains/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Properties of two bacteriocins synthesized by Leuconostoc strains</title><link>http://scien.net/chromatography/purification/properties-of-two-bacteriocins-synthesized-by-leuconostoc-strains</link> <comments>http://scien.net/chromatography/purification/properties-of-two-bacteriocins-synthesized-by-leuconostoc-strains#comments</comments> <pubDate>Sat, 11 May 2013 03:25:00 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[bacteriocins]]></category> <category><![CDATA[biosynthesized]]></category> <category><![CDATA[dextranicin]]></category> <category><![CDATA[dextranicum]]></category> <category><![CDATA[mesenterocin]]></category> <category><![CDATA[nonproducing]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/properties-of-two-bacteriocins-synthesized-by-leuconostoc-strains</guid> <description><![CDATA[Sudirman, I; Mathieu, F; Benoit, V; Lefebvre, G., 1994: Properties of two bacteriocins synthesized by Leuconostoc strains. Current microbiology 28(3): 155-159 Mesenterocin 52 (Mes-52), was produced by Leuconostoc mesenteroides ssp. mesenteroides strain Fr52 and dextranicin 24 (Dex-24) by Leuconostoc mesenteroides ssp. dextranicum strain J2 Dex-24 had a very narrow spectrum of antibacterial activity: it inhibited [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/properties-of-two-bacteriocins-synthesized-by-leuconostoc-strains/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Production of a proteinaceous phytotoxin by Ascochyta rabiei grown in expressed chickpea sap</title><link>http://scien.net/chromatography/purification/production-of-a-proteinaceous-phytotoxin-by-ascochyta-rabiei-grown-in-expressed-chickpea-sap</link> <comments>http://scien.net/chromatography/purification/production-of-a-proteinaceous-phytotoxin-by-ascochyta-rabiei-grown-in-expressed-chickpea-sap#comments</comments> <pubDate>Sat, 11 May 2013 03:19:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[czapek]]></category> <category><![CDATA[phytotoxin]]></category> <category><![CDATA[rabiei]]></category> <category><![CDATA[solanapyrone]]></category> <category><![CDATA[solanapyrones]]></category> <category><![CDATA[solidphase]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/production-of-a-proteinaceous-phytotoxin-by-ascochyta-rabiei-grown-in-expressed-chickpea-sap</guid> <description><![CDATA[Chen, Y.M.; Strange, R. N., 1994: Production of a proteinaceous phytotoxin by Ascochyta rabiei grown in expressed chickpea sap. Plant Pathology (oxford). 43(2): 321-327 Production of the solanapyrone toxins by Ascochyta rabiei is nutrient dependent. When grown on a medium consisting entirely of expressed sap from the aerial parts or young chickpea plants (Psm), only [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/production-of-a-proteinaceous-phytotoxin-by-ascochyta-rabiei-grown-in-expressed-chickpea-sap/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Production and characterization of recombinant turkey prolactin</title><link>http://scien.net/chromatography/purification/production-and-characterization-of-recombinant-turkey-prolactin</link> <comments>http://scien.net/chromatography/purification/production-and-characterization-of-recombinant-turkey-prolactin#comments</comments> <pubDate>Sat, 11 May 2013 03:18:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[tprl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/production-and-characterization-of-recombinant-turkey-prolactin</guid> <description><![CDATA[Karatzas, C. N.; Guemene, D.; Zadworny, D.; Kuhnlein, U., 1993: Production and characterization of recombinant turkey prolactin. Comparative Biochemistry &#038; Physiology B Comparative Biochemistry. 106(2): 273-280 Recombinant turkey prolactin (rctPRL) was produced as a fusion protein in E. coli, purified by affinity chromatography followed by cleavage with thrombin. The final yield of the released rctPRL [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/production-and-characterization-of-recombinant-turkey-prolactin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Primary structure of and immunoglobulin E response to the repeat subunit of gp15/400 from human lymphatic filarial parasites</title><link>http://scien.net/chromatography/purification/primary-structure-of-and-immunoglobulin-e-response-to-the-repeat-subunit-of-gp15400-from-human-lymphatic-filarial-parasites</link> <comments>http://scien.net/chromatography/purification/primary-structure-of-and-immunoglobulin-e-response-to-the-repeat-subunit-of-gp15400-from-human-lymphatic-filarial-parasites#comments</comments> <pubDate>Sat, 11 May 2013 03:16:11 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Purification]]></category> <category><![CDATA[amicrofilaremic]]></category> <category><![CDATA[elephantiasis]]></category> <category><![CDATA[microfilaremic]]></category> <category><![CDATA[pahangi]]></category><guid
isPermaLink="false">http://scien.net/chromatography/purification/primary-structure-of-and-immunoglobulin-e-response-to-the-repeat-subunit-of-gp15400-from-human-lymphatic-filarial-parasites</guid> <description><![CDATA[Paxton, William A.; Yazdanbakhsh, Maria; Kurniawan, Agnes; Partono, Felix; Maizels, Rick M.; Selkirk, Murray E., 1993: Primary structure of and immunoglobulin E response to the repeat subunit of gp15/400 from human lymphatic filarial parasites. Infection &#038; Immunity. 61(7): 2827-2833 We have isolated and sequenced clones encoding the repeated subunit of the surface-associated glycoprotein gp15/400 from [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/purification/primary-structure-of-and-immunoglobulin-e-response-to-the-repeat-subunit-of-gp15400-from-human-lymphatic-filarial-parasites/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>
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