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><channel><title>Natural Sciences Bibliography &#187; Sepharose</title> <atom:link href="http://scien.net/category/chromatography/sepharose/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>225,000 References and 150,000 Tags</description> <lastBuildDate>Sat, 25 May 2013 05:14:00 +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>Bioactivity of a pentapeptide isolated from corn gluten hydrolysate on Lolium perenne L</title><link>http://scien.net/chromatography/sepharose/bioactivity-of-a-pentapeptide-isolated-from-corn-gluten-hydrolysate-on-lolium-perenne-l</link> <comments>http://scien.net/chromatography/sepharose/bioactivity-of-a-pentapeptide-isolated-from-corn-gluten-hydrolysate-on-lolium-perenne-l#comments</comments> <pubDate>Sat, 25 May 2013 04:52:27 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/bioactivity-of-a-pentapeptide-isolated-from-corn-gluten-hydrolysate-on-lolium-perenne-l</guid> <description><![CDATA[Liu, Dl; Christians, Ne, 1996: Bioactivity of a pentapeptide isolated from corn gluten hydrolysate on Lolium perenne L. Journal of plant growth regulationer 15(1): 13-17 Corn gluten hydrolysate (Cgh) has been observed to inhibit root formation of germinating grass seeds and has the potential for use as a natural herbicide. Five dipeptides have been isolated [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/bioactivity-of-a-pentapeptide-isolated-from-corn-gluten-hydrolysate-on-lolium-perenne-l/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Attempts to purify and characterize the estrus-signalling pheromone from cow urine</title><link>http://scien.net/chromatography/sepharose/attempts-to-purify-and-characterize-the-estrus-signalling-pheromone-from-cow-urine</link> <comments>http://scien.net/chromatography/sepharose/attempts-to-purify-and-characterize-the-estrus-signalling-pheromone-from-cow-urine#comments</comments> <pubDate>Sat, 25 May 2013 04:35:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[diethylether]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/attempts-to-purify-and-characterize-the-estrus-signalling-pheromone-from-cow-urine</guid> <description><![CDATA[Dehnhard, M; Claus, R., 1996: Attempts to purify and characterize the estrus-signalling pheromone from cow urine. Theriogenology 46(1): 13-22 Attempts were undertaken to isolate and characterize the estrus specific pheromone from cow urine. All steps of the fractionation and characterization were paralleled by a bioassay with rats. Solvent extraction of estrous urine by diethylether was [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/attempts-to-purify-and-characterize-the-estrus-signalling-pheromone-from-cow-urine/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Antiviral and antiphlogistic activities of Hamamelis virginiana bark</title><link>http://scien.net/chromatography/sepharose/antiviral-and-antiphlogistic-activities-of-hamamelis-virginiana-bark</link> <comments>http://scien.net/chromatography/sepharose/antiviral-and-antiphlogistic-activities-of-hamamelis-virginiana-bark#comments</comments> <pubDate>Sat, 25 May 2013 04:09:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[antiphlogistic]]></category> <category><![CDATA[hamamelis]]></category> <category><![CDATA[hamamelitannin]]></category> <category><![CDATA[hydroalcoholic]]></category> <category><![CDATA[proanthocyanidins]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/antiviral-and-antiphlogistic-activities-of-hamamelis-virginiana-bark</guid> <description><![CDATA[Erdelmeier, C. A. J.; CinatlJ.Jr.; Rabenau, H.; Doerr, H. W.; Biber, A.; Koch, E., 1996: Antiviral and antiphlogistic activities of Hamamelis virginiana bark. Planta Medica. 62(3): 241-245 A crude hydroalcoholic extract from Hamamelis virginiana bark was subjected to ultrafiltration (Uf) with a cut-off limit of 3 kDa to obtain a higher and a lower molecular [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/antiviral-and-antiphlogistic-activities-of-hamamelis-virginiana-bark/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Antioxidant compounds from buckwheat (Fagopyrum esculentum Moench) hulls</title><link>http://scien.net/chromatography/sepharose/antioxidant-compounds-from-buckwheat-fagopyrum-esculentum-moench-hulls</link> <comments>http://scien.net/chromatography/sepharose/antioxidant-compounds-from-buckwheat-fagopyrum-esculentum-moench-hulls#comments</comments> <pubDate>Sat, 25 May 2013 04:06:38 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[dihydroxybenzaldehyde]]></category> <category><![CDATA[fagopyrum]]></category> <category><![CDATA[hyperin]]></category> <category><![CDATA[isovitexin]]></category> <category><![CDATA[peroxyl]]></category> <category><![CDATA[proanthocyanidins]]></category> <category><![CDATA[protocatechuic]]></category> <category><![CDATA[vitexin]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/antioxidant-compounds-from-buckwheat-fagopyrum-esculentum-moench-hulls</guid> <description><![CDATA[Watanabe, M.; Ohshita, Y.; Tsushida, T., 1997: Antioxidant compounds from buckwheat (Fagopyrum esculentum Moench) hulls. Journal of Agricultural and Food Chemistry 45(4): 1039-1044 Ethanolic extracts of buckwheat (Fagopyrum esculentum Moench) hulls were separated by Sephadex Lh-20 column chromatography into eight fractions. Five of the fractions exhibited peroxyl radical-scavenging activity by inhibiting the oxidation of methyl [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/antioxidant-compounds-from-buckwheat-fagopyrum-esculentum-moench-hulls/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Analysis of the green fraction of humic acids</title><link>http://scien.net/chromatography/sepharose/analysis-of-the-green-fraction-of-humic-acids</link> <comments>http://scien.net/chromatography/sepharose/analysis-of-the-green-fraction-of-humic-acids#comments</comments> <pubDate>Sat, 25 May 2013 03:49:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[dhpq]]></category> <category><![CDATA[dihydroxyperylene]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/analysis-of-the-green-fraction-of-humic-acids</guid> <description><![CDATA[Watanabe, A.; Fujimori, H.; Nagai, Y.; Miyajima, T.; Kuwatsuka, S., 1996: Analysis of the green fraction of humic acids. European Journal Of Soil Science. 47(2): 204 The green fraction of humic acids (HAs), Pg, was fractionated by gel chromatography on Sephadex G-50. Repeated chromatography of the crude Pg obtained by the first chromatography of Ha [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/analysis-of-the-green-fraction-of-humic-acids/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Actin purified from maize pollen functions in living plant cells</title><link>http://scien.net/chromatography/sepharose/actin-purified-from-maize-pollen-functions-in-living-plant-cells</link> <comments>http://scien.net/chromatography/sepharose/actin-purified-from-maize-pollen-functions-in-living-plant-cells#comments</comments> <pubDate>Fri, 24 May 2013 04:44:11 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[abps]]></category> <category><![CDATA[nonvertebrate]]></category> <category><![CDATA[profilin]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/actin-purified-from-maize-pollen-functions-in-living-plant-cells</guid> <description><![CDATA[Ren, H; Gibbon, Bc; Ashworth, Sl; Sherman, Dm; Yuan, M; Staiger, Cj, 1997: Actin purified from maize pollen functions in living plant cells. Plant cell 9(8): 1445-1457 A vast array of actin binding proteins (ABPs), together with intracellular signaling molecules, modulates the spatiotemporal distribution of actin filaments in eukaryotic cells. To investigate the complex regulation [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/actin-purified-from-maize-pollen-functions-in-living-plant-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A wound-inducible gene from Salix viminalis coding for a trypsin inhibitor</title><link>http://scien.net/chromatography/sepharose/a-wound-inducible-gene-from-salix-viminalis-coding-for-a-trypsin-inhibitor</link> <comments>http://scien.net/chromatography/sepharose/a-wound-inducible-gene-from-salix-viminalis-coding-for-a-trypsin-inhibitor#comments</comments> <pubDate>Fri, 24 May 2013 04:32:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[svti]]></category> <category><![CDATA[tataa]]></category> <category><![CDATA[viminalis]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-wound-inducible-gene-from-salix-viminalis-coding-for-a-trypsin-inhibitor</guid> <description><![CDATA[Saarikoski, P; Clapham, D; Arnold, S. Von, 1996: A wound-inducible gene from Salix viminalis coding for a trypsin inhibitor. Plant molecular biology 31(3): 465-478 A gene designated swin1.1 has been isolated by screening a Salix viminalis genomic library with a heterologous probe, win3 from Populus. The region sequenced included the entire coding sequence for a [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-wound-inducible-gene-from-salix-viminalis-coding-for-a-trypsin-inhibitor/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A novel developmental stage-specific lectin of the basidiomycete Pleurotus cornucopiae</title><link>http://scien.net/chromatography/sepharose/a-novel-developmental-stage-specific-lectin-of-the-basidiomycete-pleurotus-cornucopiae</link> <comments>http://scien.net/chromatography/sepharose/a-novel-developmental-stage-specific-lectin-of-the-basidiomycete-pleurotus-cornucopiae#comments</comments> <pubDate>Fri, 24 May 2013 03:58:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cornucopiae]]></category> <category><![CDATA[dikaryotic]]></category> <category><![CDATA[monokaryotic]]></category> <category><![CDATA[multimer]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-novel-developmental-stage-specific-lectin-of-the-basidiomycete-pleurotus-cornucopiae</guid> <description><![CDATA[Oguri, S; Ando, A; Nagata, Y., 1996: A novel developmental stage-specific lectin of the basidiomycete Pleurotus cornucopiae. Journal of bacteriology 178(19): 5692-5698 A novel lectin was isolated from mycelia of the basidiomycete Pleurotus cornucopiae grown on solid medium. The lectin was purified to homogeneity by mucin-Sepharose affinity chromatography. The molecular mass of the lectin was [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-novel-developmental-stage-specific-lectin-of-the-basidiomycete-pleurotus-cornucopiae/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A new type of staphylococcal exfoliative toxin from a Staphylococcus aureus strain isolated from a horse with phlegmon</title><link>http://scien.net/chromatography/sepharose/a-new-type-of-staphylococcal-exfoliative-toxin-from-a-staphylococcus-aureus-strain-isolated-from-a-horse-with-phlegmon</link> <comments>http://scien.net/chromatography/sepharose/a-new-type-of-staphylococcal-exfoliative-toxin-from-a-staphylococcus-aureus-strain-isolated-from-a-horse-with-phlegmon#comments</comments> <pubDate>Fri, 24 May 2013 03:56:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cellulofine]]></category> <category><![CDATA[exfoliation]]></category> <category><![CDATA[exfoliative]]></category> <category><![CDATA[hyicus]]></category> <category><![CDATA[intraepidermal]]></category> <category><![CDATA[nikolsky]]></category> <category><![CDATA[phlegmon]]></category> <category><![CDATA[seta]]></category> <category><![CDATA[setb]]></category> <category><![CDATA[setc]]></category> <category><![CDATA[shet]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-new-type-of-staphylococcal-exfoliative-toxin-from-a-staphylococcus-aureus-strain-isolated-from-a-horse-with-phlegmon</guid> <description><![CDATA[Sato, H; Matsumori, Y; Tanabe, T; Saito, H; Shimizu, A; Kawano, J., 1994: A new type of staphylococcal exfoliative toxin from a Staphylococcus aureus strain isolated from a horse with phlegmon. Infection and immunity 62(9): 3780-3785 A new type of staphylococcal exfoliative toxin (sET) was isolated from the culture filtrate of a Staphylococcus aureus strain [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-new-type-of-staphylococcal-exfoliative-toxin-from-a-staphylococcus-aureus-strain-isolated-from-a-horse-with-phlegmon/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A new procedure for the preparation of highly active melonin from the dry seeds of Cucumis melo L</title><link>http://scien.net/chromatography/sepharose/a-new-procedure-for-the-preparation-of-highly-active-melonin-from-the-dry-seeds-of-cucumis-melo-l</link> <comments>http://scien.net/chromatography/sepharose/a-new-procedure-for-the-preparation-of-highly-active-melonin-from-the-dry-seeds-of-cucumis-melo-l#comments</comments> <pubDate>Fri, 24 May 2013 03:53:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[melonin]]></category> <category><![CDATA[superdex]]></category> <category><![CDATA[unglycosylated]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-new-procedure-for-the-preparation-of-highly-active-melonin-from-the-dry-seeds-of-cucumis-melo-l</guid> <description><![CDATA[Rojo, M. A.; Arias, F. J.; Ferreras, J. M.; Iglesias, R.; Munoz, R.; Citores, L.; Jimenez, P.; Girbes, T., 1995: A new procedure for the preparation of highly active melonin from the dry seeds of Cucumis melo L. Cellular &#038; Molecular Biology (noisy-Le-Grand). 41(2): 279-287 Melon (Cucumis melo L.) dry seeds contain melonin, a protein [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-new-procedure-for-the-preparation-of-highly-active-melonin-from-the-dry-seeds-of-cucumis-melo-l/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A boron-rhamnogalacturonan-II complex from bamboo shoot cell walls</title><link>http://scien.net/chromatography/sepharose/a-boron-rhamnogalacturonan-ii-complex-from-bamboo-shoot-cell-walls</link> <comments>http://scien.net/chromatography/sepharose/a-boron-rhamnogalacturonan-ii-complex-from-bamboo-shoot-cell-walls#comments</comments> <pubDate>Fri, 24 May 2013 03:15:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[dicots]]></category> <category><![CDATA[diester]]></category> <category><![CDATA[driselase]]></category> <category><![CDATA[phyllostachys]]></category> <category><![CDATA[rhamnogalacturonan]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-boron-rhamnogalacturonan-ii-complex-from-bamboo-shoot-cell-walls</guid> <description><![CDATA[Kaneko, Satoshi; Ishii, Tadashi; Matsunaga, Toshiro, 1997: A boron-rhamnogalacturonan-II complex from bamboo shoot cell walls. Phytochemistry (oxford). 44(2): 243-248 A boron-polysaccharide complex was isolated from a Driselase digest of bamboo (Phyllostachys edulis) shoot cell walls by successive Deae Sepharose Ff, Bio-Gel P-10 and Mono Q Hr 5/5 chromatography. The complex contained 0.15% boron (w/w). The [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-boron-rhamnogalacturonan-ii-complex-from-bamboo-shoot-cell-walls/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A Lupinus albus root glycoprotein homologous to the polygalacturonase inhibitor proteins</title><link>http://scien.net/chromatography/sepharose/a-lupinus-albus-root-glycoprotein-homologous-to-the-polygalacturonase-inhibitor-proteins</link> <comments>http://scien.net/chromatography/sepharose/a-lupinus-albus-root-glycoprotein-homologous-to-the-polygalacturonase-inhibitor-proteins#comments</comments> <pubDate>Fri, 24 May 2013 03:13:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[ionically]]></category> <category><![CDATA[maior]]></category> <category><![CDATA[pgep]]></category> <category><![CDATA[pgip]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/a-lupinus-albus-root-glycoprotein-homologous-to-the-polygalacturonase-inhibitor-proteins</guid> <description><![CDATA[Costa, M. Manuela Ribeiro; Costa, Julia; Ricardo, Candido P. Pinto, 1997: A Lupinus albus root glycoprotein homologous to the polygalacturonase inhibitor proteins. Physiologia Plantarum. 99(2): 263-270 A glycoprotein with an apparent molecular mass of 42 kDa (Gp42), detected in the roots of Lupinus albus L. (cv. Rio Maior), was found to increase along the root [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/a-lupinus-albus-root-glycoprotein-homologous-to-the-polygalacturonase-inhibitor-proteins/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Tocopherols and carotenes are differently distributed in subfractions of high-density lipoprotein</title><link>http://scien.net/chromatography/sepharose/tocopherols-and-carotenes-are-differently-distributed-in-subfractions-of-high-density-lipoprotein</link> <comments>http://scien.net/chromatography/sepharose/tocopherols-and-carotenes-are-differently-distributed-in-subfractions-of-high-density-lipoprotein#comments</comments> <pubDate>Thu, 23 May 2013 05:42:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[carotenes]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/tocopherols-and-carotenes-are-differently-distributed-in-subfractions-of-high-density-lipoprotein</guid> <description><![CDATA[Brown, Andrew J.; Fragoso, Yara D., 1994: Tocopherols and carotenes are differently distributed in subfractions of high-density lipoprotein. Biochimica Et Biophysica Acta. 1210(3): 373-376 An apolipoprotein (apo) E-rich and an apo E-poor fraction of high-density lipoprotein (Hdl) were isolated from four healthy men by heparin-Sepharose affinity chromatography. On a cholesterol basis, the apo E-poor Hdl [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/tocopherols-and-carotenes-are-differently-distributed-in-subfractions-of-high-density-lipoprotein/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Thiols of Cu-treated maize plants inoculated with the arbuscular-mycorrhizal fungus Glomus intraradices</title><link>http://scien.net/chromatography/sepharose/thiols-of-cu-treated-maize-plants-inoculated-with-the-arbuscular-mycorrhizal-fungus-glomus-intraradices</link> <comments>http://scien.net/chromatography/sepharose/thiols-of-cu-treated-maize-plants-inoculated-with-the-arbuscular-mycorrhizal-fungus-glomus-intraradices#comments</comments> <pubDate>Thu, 23 May 2013 05:36:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cubp]]></category> <category><![CDATA[cubps]]></category> <category><![CDATA[glutamylcysteine]]></category> <category><![CDATA[intraradices]]></category> <category><![CDATA[nonmycorrhizal]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/thiols-of-cu-treated-maize-plants-inoculated-with-the-arbuscular-mycorrhizal-fungus-glomus-intraradices</guid> <description><![CDATA[Galli, Ulrich; Schuepp, Hannes; Brunold, Christian, 1995: Thiols of Cu-treated maize plants inoculated with the arbuscular-mycorrhizal fungus Glomus intraradices. Physiologia Plantarum. 94(2): 247-253 Mycorrhizal colonization of roots, fresh weight, content of cysteine, gamma-glutamylcysteine (gamma-Ec), glutathione (Gsh), thiol groups in Cu-binding peptides (CuBP), and the uptake of Cu were measured in roots and shoots of maize [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/thiols-of-cu-treated-maize-plants-inoculated-with-the-arbuscular-mycorrhizal-fungus-glomus-intraradices/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>The use of isolated functional heart to pharmacologically characterize active ingredients in the aqueous extracts of Mareya micrantha</title><link>http://scien.net/chromatography/sepharose/the-use-of-isolated-functional-heart-to-pharmacologically-characterize-active-ingredients-in-the-aqueous-extracts-of-mareya-micrantha</link> <comments>http://scien.net/chromatography/sepharose/the-use-of-isolated-functional-heart-to-pharmacologically-characterize-active-ingredients-in-the-aqueous-extracts-of-mareya-micrantha#comments</comments> <pubDate>Thu, 23 May 2013 05:31:53 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cardioactive]]></category> <category><![CDATA[cardiodepressant]]></category> <category><![CDATA[mareya]]></category> <category><![CDATA[micrantha]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/the-use-of-isolated-functional-heart-to-pharmacologically-characterize-active-ingredients-in-the-aqueous-extracts-of-mareya-micrantha</guid> <description><![CDATA[Guede Guina, Frederick; Tsai, Cheng S.; Smith, Margaret O.; Vangah Manda, Madelein; Washington, Benny; Ochillo, Richard F., 1995: The use of isolated functional heart to pharmacologically characterize active ingredients in the aqueous extracts of Mareya micrantha. Journal Of Ethnopharmacology. 45(1): 6 Aqueous extracts of Mareya micrantha are used as folk medicine in West Africa. However, [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/the-use-of-isolated-functional-heart-to-pharmacologically-characterize-active-ingredients-in-the-aqueous-extracts-of-mareya-micrantha/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>The separation and identification of glutathione S-transferase subunits from Orthosia gothica</title><link>http://scien.net/chromatography/sepharose/the-separation-and-identification-of-glutathione-s-transferase-subunits-from-orthosia-gothica</link> <comments>http://scien.net/chromatography/sepharose/the-separation-and-identification-of-glutathione-s-transferase-subunits-from-orthosia-gothica#comments</comments> <pubDate>Thu, 23 May 2013 05:25:38 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cdnb]]></category> <category><![CDATA[gothica]]></category> <category><![CDATA[orthosia]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/the-separation-and-identification-of-glutathione-s-transferase-subunits-from-orthosia-gothica</guid> <description><![CDATA[Egaas, Eliann; Sandvik, Morten; Svendsen, Nina O.; Skaare, Janneche U., 1995: The separation and identification of glutathione S-transferase subunits from Orthosia gothica. Insect Biochemistry &#038; Molecular Biology. 25(7): 783-788 Four subunits of the cytosolic glutathione S-transferase (Gst) in Orthosia gothica fed on willow leaves and a semisynthetic bean diet were purified as separate peaks (subunits [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/the-separation-and-identification-of-glutathione-s-transferase-subunits-from-orthosia-gothica/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>The major tuber storage protein of Araceae species is a lectin. Characterization and molecular cloning of the lectin from Arum maculatum L</title><link>http://scien.net/chromatography/sepharose/the-major-tuber-storage-protein-of-araceae-species-is-a-lectin-characterization-and-molecular-cloning-of-the-lectin-from-arum-maculatum-l</link> <comments>http://scien.net/chromatography/sepharose/the-major-tuber-storage-protein-of-araceae-species-is-a-lectin-characterization-and-molecular-cloning-of-the-lectin-from-arum-maculatum-l#comments</comments> <pubDate>Thu, 23 May 2013 05:09:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[araceae]]></category> <category><![CDATA[arum]]></category> <category><![CDATA[asialofetuin]]></category> <category><![CDATA[dieffenbachia]]></category> <category><![CDATA[sagittifolium]]></category> <category><![CDATA[schott]]></category> <category><![CDATA[sequina]]></category> <category><![CDATA[xanthosoma]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/the-major-tuber-storage-protein-of-araceae-species-is-a-lectin-characterization-and-molecular-cloning-of-the-lectin-from-arum-maculatum-l</guid> <description><![CDATA[Damme, E. J. M. van; Goossens, K.; Smeets, K.; Leuven, F. van; Verhaert, P.; Peumans, W. J., 1995: The major tuber storage protein of Araceae species is a lectin. Characterization and molecular cloning of the lectin from Arum maculatum L. Plant Physiology 107(4): 1147-1158 A new lectin was purified from tubers of Arum maculatum L. [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/the-major-tuber-storage-protein-of-araceae-species-is-a-lectin-characterization-and-molecular-cloning-of-the-lectin-from-arum-maculatum-l/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>The low-isoelectric point tyrosinase of Agaricus bisporus may be a glycoprotein</title><link>http://scien.net/chromatography/sepharose/the-low-isoelectric-point-tyrosinase-of-agaricus-bisporus-may-be-a-glycoprotein</link> <comments>http://scien.net/chromatography/sepharose/the-low-isoelectric-point-tyrosinase-of-agaricus-bisporus-may-be-a-glycoprotein#comments</comments> <pubDate>Thu, 23 May 2013 05:09:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[sporophore]]></category> <category><![CDATA[sporophores]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/the-low-isoelectric-point-tyrosinase-of-agaricus-bisporus-may-be-a-glycoprotein</guid> <description><![CDATA[Gerritsen, Yvonne A. M.; Chapelon, Chrystelle G. J.; Wichers, Harry J., 1994: The low-isoelectric point tyrosinase of Agaricus bisporus may be a glycoprotein. Phytochemistry (oxford). 35(3): 573-577 Tyrosinase (Ec 1.14.18.1) of Agaricus bisporus occurs in several isoforms that can be distinguished by their isoelectric point. The low isoelectric point (4.5) isoforms of tyrosinase from the [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/the-low-isoelectric-point-tyrosinase-of-agaricus-bisporus-may-be-a-glycoprotein/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Sucrose-sucrose fructosyltransferase in relation to fructans in developing grains of pearl millet, Pennisetum americanum</title><link>http://scien.net/chromatography/sepharose/sucrose-sucrose-fructosyltransferase-in-relation-to-fructans-in-developing-grains-of-pearl-millet-pennisetum-americanum</link> <comments>http://scien.net/chromatography/sepharose/sucrose-sucrose-fructosyltransferase-in-relation-to-fructans-in-developing-grains-of-pearl-millet-pennisetum-americanum#comments</comments> <pubDate>Wed, 22 May 2013 04:32:10 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[fructans]]></category> <category><![CDATA[fructosyltransferase]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/sucrose-sucrose-fructosyltransferase-in-relation-to-fructans-in-developing-grains-of-pearl-millet-pennisetum-americanum</guid> <description><![CDATA[Asthir, Bavita; Singh, Rangil; Gupta, A. K., 1995: Sucrose-sucrose fructosyltransferase in relation to fructans in developing grains of pearl millet, Pennisetum americanum. Indian Journal Of Experimental Biology. 33(3): 233-235 Activity of sucrose-sucrose fructosyltransferase (Sst) and contents of fructans and sucrose were determined in the developing grains of pearl millet (P. americanum). Activity of Sst was [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/sucrose-sucrose-fructosyltransferase-in-relation-to-fructans-in-developing-grains-of-pearl-millet-pennisetum-americanum/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Study on the function of cytokinin-binding protein in wheat chloroplasts</title><link>http://scien.net/chromatography/sepharose/study-on-the-function-of-cytokinin-binding-protein-in-wheat-chloroplasts</link> <comments>http://scien.net/chromatography/sepharose/study-on-the-function-of-cytokinin-binding-protein-in-wheat-chloroplasts#comments</comments> <pubDate>Wed, 22 May 2013 04:29:07 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/study-on-the-function-of-cytokinin-binding-protein-in-wheat-chloroplasts</guid> <description><![CDATA[Zhang, Hua Min; Liu, Yu; Shen, Yun Gang, 1994: Study on the function of cytokinin-binding protein in wheat chloroplasts. Acta Phytophysiologica Sinica. 20(4): 373-379 Cytokinin-binding protein (Cbp) was isolated from chloroplasts of wheat leaves and purified to a single protein by affinity chromatography on a Ba-sepharose 6b column and then used as antigen. The rabbit [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/study-on-the-function-of-cytokinin-binding-protein-in-wheat-chloroplasts/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Sensory and chemical analysis of fractions obtained by gel permeation of water-soluble Comte cheese extracts</title><link>http://scien.net/chromatography/sepharose/sensory-and-chemical-analysis-of-fractions-obtained-by-gel-permeation-of-water-soluble-comte-cheese-extracts</link> <comments>http://scien.net/chromatography/sepharose/sensory-and-chemical-analysis-of-fractions-obtained-by-gel-permeation-of-water-soluble-comte-cheese-extracts#comments</comments> <pubDate>Wed, 22 May 2013 03:31:02 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[aromas]]></category> <category><![CDATA[toyopearl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/sensory-and-chemical-analysis-of-fractions-obtained-by-gel-permeation-of-water-soluble-comte-cheese-extracts</guid> <description><![CDATA[Salles, C; Septier, C; Roudot-Algaron, F; Guillot, A; Etievant, Px, 1995: Sensory and chemical analysis of fractions obtained by gel permeation of water-soluble Comte cheese extracts. Journal of agricultural and food chemistry 43(6): 1659-1668 The pure water extraction of Comte cheese solubles and their chromatographic separation facilitate sensory analysis experiments with the fractions directly collected [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/sensory-and-chemical-analysis-of-fractions-obtained-by-gel-permeation-of-water-soluble-comte-cheese-extracts/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Selenium-containing peroxidases of germinating barley</title><link>http://scien.net/chromatography/sepharose/selenium-containing-peroxidases-of-germinating-barley</link> <comments>http://scien.net/chromatography/sepharose/selenium-containing-peroxidases-of-germinating-barley#comments</comments> <pubDate>Wed, 22 May 2013 03:29:29 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[selenoprotein]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/selenium-containing-peroxidases-of-germinating-barley</guid> <description><![CDATA[Huang, Kaixun; Lauridsen, Erling; Clausen, Jorgen, 1994: Selenium-containing peroxidases of germinating barley. Biological Trace Element Research. 46(1-2): 173-182 Germinating barley grown on an artificial medium was exposed to 75Se-selenite for 8 d. Then the leaves were homogenized and proteins were separated by means of Sephadex G-150 filtration, followed by Deae-Sepharose chromatography. Each fraction collected was [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/selenium-containing-peroxidases-of-germinating-barley/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Quaternary alkaloids from Litsea cubeba and Cryptocarya konishii</title><link>http://scien.net/chromatography/sepharose/quaternary-alkaloids-from-litsea-cubeba-and-cryptocarya-konishii</link> <comments>http://scien.net/chromatography/sepharose/quaternary-alkaloids-from-litsea-cubeba-and-cryptocarya-konishii#comments</comments> <pubDate>Tue, 21 May 2013 03:01:30 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cryptocarya]]></category> <category><![CDATA[cubeba]]></category> <category><![CDATA[formosan]]></category> <category><![CDATA[konishii]]></category> <category><![CDATA[lauraceous]]></category> <category><![CDATA[litsea]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/quaternary-alkaloids-from-litsea-cubeba-and-cryptocarya-konishii</guid> <description><![CDATA[Lee, Shoei Sheng; Lin, Yi Jean; Chen, Chien Kuang; Liu, Karin C. S.; Chen, Chung Hsiung, 1993: Quaternary alkaloids from Litsea cubeba and Cryptocarya konishii. Journal Of Natural Products (lloydia). 56(11): -1976 Centrifugal partition chromatography, Sephadex Lh-20, and ion-pair reversed-phase lc were applied in the isolation of quaternary alkaloids from two Formosan Lauraceous plants: Cryptocarya [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/quaternary-alkaloids-from-litsea-cubeba-and-cryptocarya-konishii/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II</title><link>http://scien.net/chromatography/sepharose/purification-complete-amino-acid-sequence-and-structural-characterization-of-the-heat-stable-sweet-protein-mabinlin-ii</link> <comments>http://scien.net/chromatography/sepharose/purification-complete-amino-acid-sequence-and-structural-characterization-of-the-heat-stable-sweet-protein-mabinlin-ii#comments</comments> <pubDate>Tue, 21 May 2013 02:56:34 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[capparis]]></category> <category><![CDATA[carboxamidomethylated]]></category> <category><![CDATA[levl]]></category> <category><![CDATA[mabinlin]]></category> <category><![CDATA[masaikai]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-complete-amino-acid-sequence-and-structural-characterization-of-the-heat-stable-sweet-protein-mabinlin-ii</guid> <description><![CDATA[Liu, Xiaozhu; Maeda, Shoji; Hu, Zhong; Aiuchi, Toshihiro; Nakaya, Kazuyasu; Kurihara, Yoshie, 1993: Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II. European Journal Of Biochemistry. 211(1-2): 281-287 A new sweet protein, named mabinlin Ii, was extracted with 0.5 M NaCl solution from the seeds of Capparis masaikai Levl. [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-complete-amino-acid-sequence-and-structural-characterization-of-the-heat-stable-sweet-protein-mabinlin-ii/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification, N-terminal sequencing and properties of wheat embryo acidic ribosomal A proteins with sequence similarity to calmodulin</title><link>http://scien.net/chromatography/sepharose/purification-n-terminal-sequencing-and-properties-of-wheat-embryo-acidic-ribosomal-a-proteins-with-sequence-similarity-to-calmodulin</link> <comments>http://scien.net/chromatography/sepharose/purification-n-terminal-sequencing-and-properties-of-wheat-embryo-acidic-ribosomal-a-proteins-with-sequence-similarity-to-calmodulin#comments</comments> <pubDate>Tue, 21 May 2013 02:56:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[calp]]></category> <category><![CDATA[elutes]]></category> <category><![CDATA[reactivating]]></category> <category><![CDATA[sephacel]]></category> <category><![CDATA[ultrogel]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-n-terminal-sequencing-and-properties-of-wheat-embryo-acidic-ribosomal-a-proteins-with-sequence-similarity-to-calmodulin</guid> <description><![CDATA[Polya, G. M.; Stapleton, D.; Morrice, N., 1995: Purification, N-terminal sequencing and properties of wheat embryo acidic ribosomal A proteins with sequence similarity to calmodulin. Plant Science (limerick). 105(2): 177-188 A calmodulin-like protein (Calp) was purified from wheat embryo by a procedure successively involving precipitation by trichloroacetic acid and chromatography on Deae-Sephacel, phenyl-Sepharose Cl-4b and [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-n-terminal-sequencing-and-properties-of-wheat-embryo-acidic-ribosomal-a-proteins-with-sequence-similarity-to-calmodulin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of the extracellular acidic proteases of Dichelobacter nodosus</title><link>http://scien.net/chromatography/sepharose/purification-of-the-extracellular-acidic-proteases-of-dichelobacter-nodosus</link> <comments>http://scien.net/chromatography/sepharose/purification-of-the-extracellular-acidic-proteases-of-dichelobacter-nodosus#comments</comments> <pubDate>Tue, 21 May 2013 02:56:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[dichelobacter]]></category> <category><![CDATA[footrot]]></category> <category><![CDATA[nodosus]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-of-the-extracellular-acidic-proteases-of-dichelobacter-nodosus</guid> <description><![CDATA[Kortt, Alexander A.; Burns, John E.; Vaughan, Jill A.; Stewart, David J., 1994: Purification of the extracellular acidic proteases of Dichelobacter nodosus. Biochemistry &#038; Molecular Biology International. 34(6): 1157-1166 Dichelobacter nodosus, a Gram negative obligate anaerobe and causative organism of ovine footrot, secretes a family of extracellular acidic serine proteases with pI&#8217;s in the range [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-of-the-extracellular-acidic-proteases-of-dichelobacter-nodosus/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification of a candidate gonadotropin surge inhibiting factor from porcine follicular fluid</title><link>http://scien.net/chromatography/sepharose/purification-of-a-candidate-gonadotropin-surge-inhibiting-factor-from-porcine-follicular-fluid</link> <comments>http://scien.net/chromatography/sepharose/purification-of-a-candidate-gonadotropin-surge-inhibiting-factor-from-porcine-follicular-fluid#comments</comments> <pubDate>Tue, 21 May 2013 02:56:16 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[activins]]></category> <category><![CDATA[follistatin]]></category> <category><![CDATA[follistatins]]></category> <category><![CDATA[gnsif]]></category> <category><![CDATA[immunoactivity]]></category> <category><![CDATA[inhibins]]></category> <category><![CDATA[midcycle]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-of-a-candidate-gonadotropin-surge-inhibiting-factor-from-porcine-follicular-fluid</guid> <description><![CDATA[Danforth, D. R.; Cheng, C. Y., 1995: Purification of a candidate gonadotropin surge inhibiting factor from porcine follicular fluid. Endocrinology. 136(4): 1658-1665 Several lines of evidence suggest that the ovaries of many species produce a nonsteroidal substance, termed gonadotropin surge inhibiting factor (GnSIF), which inhibits the midcycle gonadotropin surge and attenuates the pituitary response to [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-of-a-candidate-gonadotropin-surge-inhibiting-factor-from-porcine-follicular-fluid/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and some properties of sodom-apple latex proteinases</title><link>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-sodom-apple-latex-proteinases</link> <comments>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-sodom-apple-latex-proteinases#comments</comments> <pubDate>Tue, 21 May 2013 02:56:11 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[azocoll]]></category> <category><![CDATA[sodom]]></category> <category><![CDATA[superdex]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-some-properties-of-sodom-apple-latex-proteinases</guid> <description><![CDATA[Aworh, O. C.; Kasche, V.; Apampa, O. O., 1994: Purification and some properties of sodom-apple latex proteinases. Food Chemistry. 50(4): 359-362 Two thiol-activated proteinases with isoelectric points (pIs approximately 9-9.5) were purified from sodom-apple latex by chromatography on Q-Sepharose and Superdex 200. Proteinase I had an estimated molecular weight of approximately 25,000 and proteinase Ii [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-sodom-apple-latex-proteinases/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and some properties of Phaseolus mungo lectin</title><link>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-phaseolus-mungo-lectin</link> <comments>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-phaseolus-mungo-lectin#comments</comments> <pubDate>Tue, 21 May 2013 02:56:10 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[galactosen]]></category> <category><![CDATA[trypsinized]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-some-properties-of-phaseolus-mungo-lectin</guid> <description><![CDATA[Sharma, Sadhana; Salahuddin, Ahmad, 1993: Purification and some properties of Phaseolus mungo lectin. Journal Of Agricultural &#038; Food Chemistry. 41(5): 700-703 Phaseolus mungo lectin in pure form was isolated from seeds by affinity chromatography on a galactosyl Sepharose 6b column. The lectin contained 8.3% neutral carbohydrate. It absorbed maximally near 278 nm, and the corresponding [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-some-properties-of-phaseolus-mungo-lectin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and partial characterization of an induced antibacterial protein in the silkworm, Bombyx mori</title><link>http://scien.net/chromatography/sepharose/purification-and-partial-characterization-of-an-induced-antibacterial-protein-in-the-silkworm-bombyx-mori</link> <comments>http://scien.net/chromatography/sepharose/purification-and-partial-characterization-of-an-induced-antibacterial-protein-in-the-silkworm-bombyx-mori#comments</comments> <pubDate>Tue, 21 May 2013 02:56:00 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[lysozymes]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-partial-characterization-of-an-induced-antibacterial-protein-in-the-silkworm-bombyx-mori</guid> <description><![CDATA[Abraham, E. G.; Nagaraju, J.; Salunke, D.; Gupta, H. M.; Datta, R. K., 1995: Purification and partial characterization of an induced antibacterial protein in the silkworm, Bombyx mori. Journal Of Invertebrate Pathology. 65(1): 17-24 Injection of live Escherichia coli into larvae of the silkworm, Bombyx mori, induces antibacterial activity in the hemolymph. The major induced [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-partial-characterization-of-an-induced-antibacterial-protein-in-the-silkworm-bombyx-mori/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of vitellin-2 from the ovary of the American cockroach, Periplaneta americana</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-vitellin-2-from-the-ovary-of-the-american-cockroach-periplaneta-americana</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-vitellin-2-from-the-ovary-of-the-american-cockroach-periplaneta-americana#comments</comments> <pubDate>Tue, 21 May 2013 02:55:43 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[anechura]]></category> <category><![CDATA[cletus]]></category> <category><![CDATA[dermaptera]]></category> <category><![CDATA[ducetia]]></category> <category><![CDATA[fulginosa]]></category> <category><![CDATA[illustris]]></category> <category><![CDATA[schmidti]]></category> <category><![CDATA[vitellins]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-vitellin-2-from-the-ovary-of-the-american-cockroach-periplaneta-americana</guid> <description><![CDATA[Kim, Hak R.; Lee, Sand Dae, 1994: Purification and characterization of vitellin-2 from the ovary of the American cockroach, Periplaneta americana. Comparative Biochemistry &#038; Physiology B Comparative Biochemistry &#038; Molecular Biology. 108(1): 135-145 Two vitellins (Vn-1 and Vn-2) were identified in cockroach ovary. Vn-2 was purified by ion-exchange chromatography using Deae cellulose and Sepharose Cl-6b, [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-vitellin-2-from-the-ovary-of-the-american-cockroach-periplaneta-americana/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-plantaricin-a-a-lactobacillus-plantarum-bacteriocin-whose-activity-depends-on-the-action-of-two-peptides</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-plantaricin-a-a-lactobacillus-plantarum-bacteriocin-whose-activity-depends-on-the-action-of-two-peptides#comments</comments> <pubDate>Tue, 21 May 2013 02:55:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[plantaricin]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-plantaricin-a-a-lactobacillus-plantarum-bacteriocin-whose-activity-depends-on-the-action-of-two-peptides</guid> <description><![CDATA[Nissen Meyer, Jon; Larsen, Annette Granly; Sletten, Knut; Daeschel, Mark; Nes, Ingolf F., 1993: Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides. Journal Of General Microbiology. 139(9): -1978 A Lactobacillus plantarum bacteriocin, plantaricin A, has been purified to homogeneity by ammonium sulphate precipitation, binding [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-plantaricin-a-a-lactobacillus-plantarum-bacteriocin-whose-activity-depends-on-the-action-of-two-peptides/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of pectin methylesterases from mung bean hypocotyl cell walls</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-pectin-methylesterases-from-mung-bean-hypocotyl-cell-walls</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-pectin-methylesterases-from-mung-bean-hypocotyl-cell-walls#comments</comments> <pubDate>Tue, 21 May 2013 02:55:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[methylesterase]]></category> <category><![CDATA[methylesterases]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-pectin-methylesterases-from-mung-bean-hypocotyl-cell-walls</guid> <description><![CDATA[Bordenave, M.; Goldberg, R., 1993: Purification and characterization of pectin methylesterases from mung bean hypocotyl cell walls. Phytochemistry (oxford). 33(5): 999-1003 A saline eluate of Mung bean hypocotyl cell walls was submitted to carboxy-methyl Sepharose chromatography. Detection of pectin methylesterase (Pme) activities after Ief of the active fractions revealed the occurrence of at least four [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-pectin-methylesterases-from-mung-bean-hypocotyl-cell-walls/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of nitrate reductase isozymes from Brassica campestris leaves</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-nitrate-reductase-isozymes-from-brassica-campestris-leaves</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-nitrate-reductase-isozymes-from-brassica-campestris-leaves#comments</comments> <pubDate>Tue, 21 May 2013 02:55:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[cnrs]]></category> <category><![CDATA[inrs]]></category> <category><![CDATA[microheterogeneity]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-nitrate-reductase-isozymes-from-brassica-campestris-leaves</guid> <description><![CDATA[Ling, Jun; Tang, Yu Wei; Shi, Jiao Nai, 1994: Purification and characterization of nitrate reductase isozymes from Brassica campestris leaves. Acta Phytophysiologica Sinica. 20(1): 31-38 It has been known that there are mainly two types of nitrate reductase (Nr) isozymes, inducible Nr (iNR) and constitutive Nr (cNR), in higher plants. Although iNR has been thoroughly [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-nitrate-reductase-isozymes-from-brassica-campestris-leaves/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of apolipophorin-III from haemolymph of fall webworm Hyphantria cunea Drury</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-apolipophorin-iii-from-haemolymph-of-fall-webworm-hyphantria-cunea-drury</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-apolipophorin-iii-from-haemolymph-of-fall-webworm-hyphantria-cunea-drury#comments</comments> <pubDate>Tue, 21 May 2013 02:55:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[apolipophorin]]></category> <category><![CDATA[apolp]]></category> <category><![CDATA[cunea]]></category> <category><![CDATA[drury]]></category> <category><![CDATA[hyphantria]]></category> <category><![CDATA[webworm]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-apolipophorin-iii-from-haemolymph-of-fall-webworm-hyphantria-cunea-drury</guid> <description><![CDATA[Yun, Hwa Kyung; Seo, Sin Ja; Kim, Hak Ryul, 1994: Purification and characterization of apolipophorin-III from haemolymph of fall webworm Hyphantria cunea Drury. Korean Journal Of Zoology. 37(4): 488-494 Apolipophorin-Iii (ApoLp-Iii) was purified from adult hemolymph of Hyphantria cunea and their molecular weight and synthetic place were investigated. ApoLp-Iii purification was performed by KBr-density gradient [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-apolipophorin-iii-from-haemolymph-of-fall-webworm-hyphantria-cunea-drury/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of an N-acetyllactosamine-specific lectin from tubers of Arum maculatum</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-tubers-of-arum-maculatum</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-tubers-of-arum-maculatum#comments</comments> <pubDate>Tue, 21 May 2013 02:55:22 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[acetyllactosamine]]></category> <category><![CDATA[araceae]]></category> <category><![CDATA[arum]]></category> <category><![CDATA[asialoglycoproteins]]></category> <category><![CDATA[biose]]></category> <category><![CDATA[chitobiose]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-tubers-of-arum-maculatum</guid> <description><![CDATA[Allen, Anthony K., 1995: Purification and characterization of an N-acetyllactosamine-specific lectin from tubers of Arum maculatum. Biochimica Et Biophysica Acta. 1244(1): 129-132 A lectin was purified from the tubers of Arum maculatum (family Araceae) by affinity chromatography on a thyroglobulin-Sepharose column. The lectin is not a glycoprotein and has a subunit molecular weight of 14 [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-an-n-acetyllactosamine-specific-lectin-from-tubers-of-arum-maculatum/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a thermostable glucoamylase from a Myrothecium isolate</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-thermostable-glucoamylase-from-a-myrothecium-isolate</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-thermostable-glucoamylase-from-a-myrothecium-isolate#comments</comments> <pubDate>Tue, 21 May 2013 02:55:19 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[gluc]]></category> <category><![CDATA[glucoamylases]]></category> <category><![CDATA[myrothecium]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-thermostable-glucoamylase-from-a-myrothecium-isolate</guid> <description><![CDATA[Ali, Showkat; Malek, S.; Hossain, Z., 1994: Purification and characterization of a thermostable glucoamylase from a Myrothecium isolate. Journal Of Applied Bacteriology. 76(3): 210-215 Two glucoamylases, gluc I and gluc Ii, were purified to homogeneity from the culture filtrate of a Myrothecium strain M1 by chromatography on Deae-cellulose and concanavalin A-sepharose. Molecular masses deduced by [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-thermostable-glucoamylase-from-a-myrothecium-isolate/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-phosphatidylinositol-4-kinase-activator-in-carrot-cells</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-phosphatidylinositol-4-kinase-activator-in-carrot-cells#comments</comments> <pubDate>Tue, 21 May 2013 02:55:18 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-phosphatidylinositol-4-kinase-activator-in-carrot-cells</guid> <description><![CDATA[Yang, W; Burkhart, W; Cavallius, J; Merrick, Wc; Boss, Wf, 1993: Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells. Journal of biological chemistry 268(1): 392-398 A phosphatidylinositol 4-kinase activator (Plk-A49) has been purified from carrot cells grown in suspension culture. The activator was purified from a soluble fraction using Deae-Sepharose Cl-6b and [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-phosphatidylinositol-4-kinase-activator-in-carrot-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a new 120 kDa alkaline proteinase of Trypanosoma cruzi</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-new-120-kda-alkaline-proteinase-of-trypanosoma-cruzi</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-new-120-kda-alkaline-proteinase-of-trypanosoma-cruzi#comments</comments> <pubDate>Tue, 21 May 2013 02:55:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[glutaryl]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-new-120-kda-alkaline-proteinase-of-trypanosoma-cruzi</guid> <description><![CDATA[Santana, Jaime Martins; Grellier, Philippe; Rodier, Marie Helene; Schrevel, Joseph; Teixeira, Antonio, 1992: Purification and characterization of a new 120 kDa alkaline proteinase of Trypanosoma cruzi. Biochemical &#038; Biophysical Research Communications. 187(3): 1466-1473 A new alkaline proteinase activity was identified in cell-free extracts of Trypanosoma cruzi epimastigotes on the basis of its ability to hydrolyze [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-new-120-kda-alkaline-proteinase-of-trypanosoma-cruzi/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of a low molecular mass cysteine proteinase inhibitor from bovine colostrum</title><link>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-low-molecular-mass-cysteine-proteinase-inhibitor-from-bovine-colostrum</link> <comments>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-low-molecular-mass-cysteine-proteinase-inhibitor-from-bovine-colostrum#comments</comments> <pubDate>Tue, 21 May 2013 02:55:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Sepharose]]></category> <category><![CDATA[gelfiltration]]></category> <category><![CDATA[superdex]]></category><guid
isPermaLink="false">http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-low-molecular-mass-cysteine-proteinase-inhibitor-from-bovine-colostrum</guid> <description><![CDATA[Kirihara, Osamu; Ohishi, Hifumi; Hosono, Akiyoshi, 1995: Purification and characterization of a low molecular mass cysteine proteinase inhibitor from bovine colostrum. Lebensmittel-Wissenschaft &#038; Technologie. 28(5): 495-500 A new type of cysteine proteinase inhibitor was purified from bovine colostrum by affinity chromatography using papain-sepharose column and gelfiltration chromatography on Superdex-7 The purified inhibitor showed a single [...]]]></description> <wfw:commentRss>http://scien.net/chromatography/sepharose/purification-and-characterization-of-a-low-molecular-mass-cysteine-proteinase-inhibitor-from-bovine-colostrum/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>