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><channel><title>Natural Sciences Bibliography &#187; Enzyme</title> <atom:link href="http://scien.net/category/enzyme/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>Subcellular location of lincomycin resistance in Nicotiana mutants</title><link>http://scien.net/enzyme/subcellular-location-of-lincomycin-resistance-in-nicotiana-mutants</link> <comments>http://scien.net/enzyme/subcellular-location-of-lincomycin-resistance-in-nicotiana-mutants#comments</comments> <pubDate>Sat, 11 May 2013 06:05:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[cybrid]]></category> <category><![CDATA[plumbaginifolia]]></category> <category><![CDATA[undulata]]></category><guid
isPermaLink="false">http://scien.net/enzyme/subcellular-location-of-lincomycin-resistance-in-nicotiana-mutants</guid> <description><![CDATA[Cseplo, A; Eigel, L; Horvath, Gv; Medgyesy, P; Herrmann, Rg; Koop, Hu, 1993: Subcellular location of lincomycin resistance in Nicotiana mutants. M G G: Molecular and general genetics 236(2-3): 163-170 Lincomycin-resistant Nicotiana plumbaginifolia plastid mutants were considered also to carry mitochondrial mutations on the basis of their ability to grow in the dark under selective [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/subcellular-location-of-lincomycin-resistance-in-nicotiana-mutants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Subcellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus and Tabernaemontana divaricata</title><link>http://scien.net/enzyme/subcellular-localization-of-tryptophan-decarboxylase-strictosidine-synthase-and-strictosidine-glucosidase-in-suspension-cultured-cells-of-catharanthus-roseus-and-tabernaemontana-divaricata</link> <comments>http://scien.net/enzyme/subcellular-localization-of-tryptophan-decarboxylase-strictosidine-synthase-and-strictosidine-glucosidase-in-suspension-cultured-cells-of-catharanthus-roseus-and-tabernaemontana-divaricata#comments</comments> <pubDate>Sat, 11 May 2013 06:05:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[divaricata]]></category> <category><![CDATA[roem]]></category> <category><![CDATA[schult]]></category> <category><![CDATA[secologanin]]></category> <category><![CDATA[strictosidine]]></category> <category><![CDATA[tabernaemontana]]></category><guid
isPermaLink="false">http://scien.net/enzyme/subcellular-localization-of-tryptophan-decarboxylase-strictosidine-synthase-and-strictosidine-glucosidase-in-suspension-cultured-cells-of-catharanthus-roseus-and-tabernaemontana-divaricata</guid> <description><![CDATA[Stevens, Lh; Blom, Tjm; Verpoorte, R., 1993: Subcellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus and Tabernaemontana divaricata. Plant cell reports2(10): 573-576 The subcellular localization of tryptophan decarboxylase, strictosidine synthase and strictosidine glucosidase in suspension cultured cells of Catharanthus roseus (L.) G. Don and Tabernaemontana divaricata [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/subcellular-localization-of-tryptophan-decarboxylase-strictosidine-synthase-and-strictosidine-glucosidase-in-suspension-cultured-cells-of-catharanthus-roseus-and-tabernaemontana-divaricata/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Subcellular distribution of superoxide dismutase and catalase in human malarial parasite Plasmodium vivax</title><link>http://scien.net/enzyme/subcellular-distribution-of-superoxide-dismutase-and-catalase-in-human-malarial-parasite-plasmodium-vivax</link> <comments>http://scien.net/enzyme/subcellular-distribution-of-superoxide-dismutase-and-catalase-in-human-malarial-parasite-plasmodium-vivax#comments</comments> <pubDate>Sat, 11 May 2013 06:05:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category><guid
isPermaLink="false">http://scien.net/enzyme/subcellular-distribution-of-superoxide-dismutase-and-catalase-in-human-malarial-parasite-plasmodium-vivax</guid> <description><![CDATA[Sharma, Arun, 1993: Subcellular distribution of superoxide dismutase and catalase in human malarial parasite Plasmodium vivax. Indian Journal Of Experimental Biology. 31(3): 275-277 Endogenous superoxide dismutase (Sod) has not been found to be present in Plasmodium vivax, a human malarial parasite and therefore it adopts and concentrates Sod from the host cell erythrocytes. It is [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/subcellular-distribution-of-superoxide-dismutase-and-catalase-in-human-malarial-parasite-plasmodium-vivax/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Subcellular distribution of O-acetylserine(thiol)lyase in cauliflower (Brassica oleracea L.) inflorescence</title><link>http://scien.net/enzyme/subcellular-distribution-of-o-acetylserinethiollyase-in-cauliflower-brassica-oleracea-l-inflorescence</link> <comments>http://scien.net/enzyme/subcellular-distribution-of-o-acetylserinethiollyase-in-cauliflower-brassica-oleracea-l-inflorescence#comments</comments> <pubDate>Sat, 11 May 2013 06:05:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[acetylserinethiollyas]]></category> <category><![CDATA[nongreen]]></category> <category><![CDATA[proplastids]]></category><guid
isPermaLink="false">http://scien.net/enzyme/subcellular-distribution-of-o-acetylserinethiollyase-in-cauliflower-brassica-oleracea-l-inflorescence</guid> <description><![CDATA[Rolland, N.; Droux, M.; Douce, R., 1992: Subcellular distribution of O-acetylserine(thiol)lyase in cauliflower (Brassica oleracea L.) inflorescence. Plant Physiology 98(3): 927-935 The subcellular localization of O-acetylserine(thiol)lyase (Ec 4.2.99.8) in nongreen tissue from higher plants has been studied using purified proplastids, mitochondria, and protoplasts from cauliflower (Brassica oleracea L.) buds as a source of subcellular fractions. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/subcellular-distribution-of-o-acetylserinethiollyase-in-cauliflower-brassica-oleracea-l-inflorescence/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Subcellular and immunocytochemical localization of the enzymes involved in ammonia assimilation in mesophyll and bundle-sheath cells of maize leaves</title><link>http://scien.net/enzyme/reductase/subcellular-and-immunocytochemical-localization-of-the-enzymes-involved-in-ammonia-assimilation-in-mesophyll-and-bundle-sheath-cells-of-maize-leaves</link> <comments>http://scien.net/enzyme/reductase/subcellular-and-immunocytochemical-localization-of-the-enzymes-involved-in-ammonia-assimilation-in-mesophyll-and-bundle-sheath-cells-of-maize-leaves#comments</comments> <pubDate>Sat, 11 May 2013 06:05:54 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Reductase]]></category> <category><![CDATA[gogat]]></category> <category><![CDATA[photorespiratory]]></category><guid
isPermaLink="false">http://scien.net/enzyme/reductase/subcellular-and-immunocytochemical-localization-of-the-enzymes-involved-in-ammonia-assimilation-in-mesophyll-and-bundle-sheath-cells-of-maize-leaves</guid> <description><![CDATA[Becker, Tw; Perrot-Rechenmann, C; Suzuki, A; Hirel, B., 1993: Subcellular and immunocytochemical localization of the enzymes involved in ammonia assimilation in mesophyll and bundle-sheath cells of maize leaves. Planta 91(1): 129-136 The cellular localization of the enzymes involved in primary nitrogen assimilation was investigated following separation of mesophyll protoplasts and bundle-sheath cells of maize (Zea [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/reductase/subcellular-and-immunocytochemical-localization-of-the-enzymes-involved-in-ammonia-assimilation-in-mesophyll-and-bundle-sheath-cells-of-maize-leaves/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Subacute toxicity of T-2 toxin and DAS in broiler chicks</title><link>http://scien.net/enzyme/subacute-toxicity-of-t-2-toxin-and-das-in-broiler-chicks</link> <comments>http://scien.net/enzyme/subacute-toxicity-of-t-2-toxin-and-das-in-broiler-chicks#comments</comments> <pubDate>Sat, 11 May 2013 06:05:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[diacetoxyscirpenol]]></category> <category><![CDATA[hybro]]></category> <category><![CDATA[inconsistently]]></category> <category><![CDATA[pathohistological]]></category><guid
isPermaLink="false">http://scien.net/enzyme/subacute-toxicity-of-t-2-toxin-and-das-in-broiler-chicks</guid> <description><![CDATA[Grabarevic, Z.; Nemanic, Ankica; Jagic, V.; Tisljar, Marina; Artukovic, Branka; Dzaja, P.; Culjak, K.; Rinck, I., 1992: Subacute toxicity of T-2 toxin and DAS in broiler chicks. Veterinarski Arhiv. 62(6): 317-324 Three groups containing 30 one-day-old Hybro broiler chicks each were used in the experiment. Group K was control, group B received 0.5 ppm of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/subacute-toxicity-of-t-2-toxin-and-das-in-broiler-chicks/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studying some properties of amylases extracted from d Anjou pears</title><link>http://scien.net/enzyme/studying-some-properties-of-amylases-extracted-from-d-anjou-pears</link> <comments>http://scien.net/enzyme/studying-some-properties-of-amylases-extracted-from-d-anjou-pears#comments</comments> <pubDate>Sat, 11 May 2013 06:05:46 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[anjou]]></category> <category><![CDATA[danjou]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studying-some-properties-of-amylases-extracted-from-d-anjou-pears</guid> <description><![CDATA[Li, S. J.; Facteau, T. J.; Chen, P., 1993: Studying some properties of amylases extracted from d Anjou pears. HortScience 28(4): 317-319 Several characteristics of amylases involved in starch degradation were studied in extracts from immature (30 days before harvest) &#8216;d&#8217;Anjou&#8217; pears (Pyrus communis L.). Enzyme activity was not detected until after at least 60 [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studying-some-properties-of-amylases-extracted-from-d-anjou-pears/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process</title><link>http://scien.net/enzyme/study-of-the-enzymatic-hydrolysis-of-cellulose-for-production-of-fuel-ethanol-by-the-simultaneous-saccharification-and-fermentation-process</link> <comments>http://scien.net/enzyme/study-of-the-enzymatic-hydrolysis-of-cellulose-for-production-of-fuel-ethanol-by-the-simultaneous-saccharification-and-fermentation-process#comments</comments> <pubDate>Sat, 11 May 2013 06:05:00 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[ethanologenic]]></category> <category><![CDATA[saccharification]]></category><guid
isPermaLink="false">http://scien.net/enzyme/study-of-the-enzymatic-hydrolysis-of-cellulose-for-production-of-fuel-ethanol-by-the-simultaneous-saccharification-and-fermentation-process</guid> <description><![CDATA[Philippidis, George P.; Smith, Tammy K.; Wyman, Charles E., 1993: Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process. Biotechnology &#038; Bioengineering. 41(9): 846-853 The biochemical conversion of cellulosic biomass to ethanol, a promising alternative fuel, can be carried out efficiently and economically using the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/study-of-the-enzymatic-hydrolysis-of-cellulose-for-production-of-fuel-ethanol-by-the-simultaneous-saccharification-and-fermentation-process/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Study of multiplication of cucumber mosaic virus in susceptible and resistant Capsicum annuum lines</title><link>http://scien.net/enzyme/immunosorbent/study-of-multiplication-of-cucumber-mosaic-virus-in-susceptible-and-resistant-capsicum-annuum-lines</link> <comments>http://scien.net/enzyme/immunosorbent/study-of-multiplication-of-cucumber-mosaic-virus-in-susceptible-and-resistant-capsicum-annuum-lines#comments</comments> <pubDate>Sat, 11 May 2013 06:04:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Immunosorbent]]></category> <category><![CDATA[vania]]></category> <category><![CDATA[yolo]]></category><guid
isPermaLink="false">http://scien.net/enzyme/immunosorbent/study-of-multiplication-of-cucumber-mosaic-virus-in-susceptible-and-resistant-capsicum-annuum-lines</guid> <description><![CDATA[Nono Womdim, R.; Gebre Selassie, K.; Palloix, A.; Pochard, E.; Marchoux, G., 1993: Study of multiplication of cucumber mosaic virus in susceptible and resistant Capsicum annuum lines. Annals Of Applied Biology. 122(1): 49-56 A previous survey on pepper lines (Capsicum annuum L.) indicated that a susceptible cultivar, Yolo Wonder, reacted to cucumber mosaic virus (Cmv) [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/immunosorbent/study-of-multiplication-of-cucumber-mosaic-virus-in-susceptible-and-resistant-capsicum-annuum-lines/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Study of mechanism of lipolysis inhibition by bovine milk proteose-peptone component 3</title><link>http://scien.net/enzyme/study-of-mechanism-of-lipolysis-inhibition-by-bovine-milk-proteose-peptone-component-3</link> <comments>http://scien.net/enzyme/study-of-mechanism-of-lipolysis-inhibition-by-bovine-milk-proteose-peptone-component-3#comments</comments> <pubDate>Sat, 11 May 2013 06:04:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[colipase]]></category> <category><![CDATA[proteose]]></category> <category><![CDATA[taurodeoxycholate]]></category> <category><![CDATA[tensiometric]]></category> <category><![CDATA[tetradecane]]></category> <category><![CDATA[tributyrin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/study-of-mechanism-of-lipolysis-inhibition-by-bovine-milk-proteose-peptone-component-3</guid> <description><![CDATA[Girardet, Jean Michel; Linden, Guy; Loye, Sylvie; Courthaudon, Jean Luc; Lorient, Denis, 1993: Study of mechanism of lipolysis inhibition by bovine milk proteose-peptone component 3. Journal Of Dairy Science. 76(8): 2156-2163 Milk component 3 was an inhibitor of lipoprotein lipase activity responsible for spontaneous lipolysis occurring in milk stored at 4 degree C. Experiments using [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/study-of-mechanism-of-lipolysis-inhibition-by-bovine-milk-proteose-peptone-component-3/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Study of acetoin reductase from Kluyveromyces marxianus</title><link>http://scien.net/enzyme/reductase/study-of-acetoin-reductase-from-kluyveromyces-marxianus</link> <comments>http://scien.net/enzyme/reductase/study-of-acetoin-reductase-from-kluyveromyces-marxianus#comments</comments> <pubDate>Sat, 11 May 2013 06:04:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Reductase]]></category> <category><![CDATA[acetoin]]></category> <category><![CDATA[butanediol]]></category> <category><![CDATA[marxianus]]></category><guid
isPermaLink="false">http://scien.net/enzyme/reductase/study-of-acetoin-reductase-from-kluyveromyces-marxianus</guid> <description><![CDATA[Schwarz, J. G.; Hang, Y. D., 1993: Study of acetoin reductase from Kluyveromyces marxianus. Letters In Applied Microbiology. 16(1): 14-16 Acetoin reductase (Ec 1.1.1.4) from Kluyveromyces marxianus var. marxianus Nrrl Y-1196 was found to possess the highest specific activity (3.64 units/mg protein) of the four cultures studied. The enzyme was Nadh-dependent and catalyzed the conversion [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/reductase/study-of-acetoin-reductase-from-kluyveromyces-marxianus/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on the substrate specificity of a peptide amidase partially purified from orange flavedo</title><link>http://scien.net/enzyme/peptide/studies-on-the-substrate-specificity-of-a-peptide-amidase-partially-purified-from-orange-flavedo</link> <comments>http://scien.net/enzyme/peptide/studies-on-the-substrate-specificity-of-a-peptide-amidase-partially-purified-from-orange-flavedo#comments</comments> <pubDate>Sat, 11 May 2013 06:04:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Peptide]]></category> <category><![CDATA[angew]]></category> <category><![CDATA[deamidated]]></category> <category><![CDATA[deamidation]]></category> <category><![CDATA[engl]]></category> <category><![CDATA[flavedo]]></category> <category><![CDATA[kula]]></category><guid
isPermaLink="false">http://scien.net/enzyme/peptide/studies-on-the-substrate-specificity-of-a-peptide-amidase-partially-purified-from-orange-flavedo</guid> <description><![CDATA[Kammermeier Steinke, D.; Schwarz, A.; Wandrey, C.; Kula, M. R., 1993: Studies on the substrate specificity of a peptide amidase partially purified from orange flavedo. Enzyme &#038; Microbial Technology. 15(9): 764-769 We recently reported the isolation and some properties of an unusual enzyme called peptide amidase (Steinke, D. and Kula, M. R. Angew. Chem. Int. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/peptide/studies-on-the-substrate-specificity-of-a-peptide-amidase-partially-purified-from-orange-flavedo/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on the proteolytic enzymes of potato tuber</title><link>http://scien.net/enzyme/studies-on-the-proteolytic-enzymes-of-potato-tuber</link> <comments>http://scien.net/enzyme/studies-on-the-proteolytic-enzymes-of-potato-tuber#comments</comments> <pubDate>Sat, 11 May 2013 06:03:53 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[catalizes]]></category> <category><![CDATA[phmb]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studies-on-the-proteolytic-enzymes-of-potato-tuber</guid> <description><![CDATA[Isola, Maria C.; Franzoni, Luis, 1993: Studies on the proteolytic enzymes of potato tuber. Plant Physiology &#038; Biochemistry (montrouge). 31(2): 169-174 An endopeptidase was separated by gel filtration from potato tuber (Solanum tuberosum L.) corresponding to a molecular mass of about 25 kDa. The enzyme catalizes the proteolytic cleavage of gelatin, is stimulated by mercaptoethanol [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studies-on-the-proteolytic-enzymes-of-potato-tuber/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on the mercury volatilizing enzymes in nitrogen-fixing Beijerinckia mobilis</title><link>http://scien.net/enzyme/reductase/studies-on-the-mercury-volatilizing-enzymes-in-nitrogen-fixing-beijerinckia-mobilis</link> <comments>http://scien.net/enzyme/reductase/studies-on-the-mercury-volatilizing-enzymes-in-nitrogen-fixing-beijerinckia-mobilis#comments</comments> <pubDate>Sat, 11 May 2013 06:03:45 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Reductase]]></category> <category><![CDATA[agno]]></category> <category><![CDATA[beijerinckia]]></category> <category><![CDATA[bino]]></category> <category><![CDATA[cocl]]></category> <category><![CDATA[cuso]]></category> <category><![CDATA[mobilis]]></category> <category><![CDATA[organomercurial]]></category> <category><![CDATA[volatilizing]]></category><guid
isPermaLink="false">http://scien.net/enzyme/reductase/studies-on-the-mercury-volatilizing-enzymes-in-nitrogen-fixing-beijerinckia-mobilis</guid> <description><![CDATA[Ray, S.; Pahan, K.; Gachhui, R.; Chaudhuri, J.; Mandal, A., 1993: Studies on the mercury volatilizing enzymes in nitrogen-fixing Beijerinckia mobilis. World Journal Of Microbiology &#038; Biotechnology. 9(2): 184-186 Beijerinckia mobilis KDr-2, a broad-spectrum, mercury-resistant nitrogen-fixing organism, possesses multiple metal-resistance properties. Mercuric reductase and organomercurial lyase activities of this bacterial strain were determined using different [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/reductase/studies-on-the-mercury-volatilizing-enzymes-in-nitrogen-fixing-beijerinckia-mobilis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on the growth of a thermotolerant yeast strain, Kluyveromyces marxianus IMB3, on sucrose containing media</title><link>http://scien.net/enzyme/studies-on-the-growth-of-a-thermotolerant-yeast-strain-kluyveromyces-marxianus-imb3-on-sucrose-containing-media</link> <comments>http://scien.net/enzyme/studies-on-the-growth-of-a-thermotolerant-yeast-strain-kluyveromyces-marxianus-imb3-on-sucrose-containing-media#comments</comments> <pubDate>Sat, 11 May 2013 06:03:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[marxianus]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studies-on-the-growth-of-a-thermotolerant-yeast-strain-kluyveromyces-marxianus-imb3-on-sucrose-containing-media</guid> <description><![CDATA[Fleming, M; Barron, N; Mchale, L; Marchant, R; Mchale, Ap, 1993: Studies on the growth of a thermotolerant yeast strain, Kluyveromyces marxianus IMB3, on sucrose containing media. Biotechnology letters 15(12): 1195-1198 A thermotolerant alcohol-producing yeast strain, Kluyveromyces marxianus Imb3 was shown to grow on sucrose (10%) containing media at 45 degrees C. Under such conditions [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studies-on-the-growth-of-a-thermotolerant-yeast-strain-kluyveromyces-marxianus-imb3-on-sucrose-containing-media/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts</title><link>http://scien.net/enzyme/escherichia/studies-on-the-expression-of-ndh-h-a-subunit-of-the-nadph-plastoquinone-oxidoreductase-of-higher-plant-chloroplasts</link> <comments>http://scien.net/enzyme/escherichia/studies-on-the-expression-of-ndh-h-a-subunit-of-the-nadph-plastoquinone-oxidoreductase-of-higher-plant-chloroplasts#comments</comments> <pubDate>Sat, 11 May 2013 06:03:09 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[atpadp]]></category> <category><![CDATA[etioplasts]]></category> <category><![CDATA[nadphnadp]]></category> <category><![CDATA[ndha]]></category> <category><![CDATA[ndhi]]></category> <category><![CDATA[ndhk]]></category> <category><![CDATA[plastoquinone]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/studies-on-the-expression-of-ndh-h-a-subunit-of-the-nadph-plastoquinone-oxidoreductase-of-higher-plant-chloroplasts</guid> <description><![CDATA[Berger, S.; Ellersiek, U.; Westhoff, P.; Steinmuller, K., 1993: Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts. Planta 190(1): 25-31 The plastid genomes of higher plants contain eleven reading frames (ndhA-K) that are homologous to genes encoding subunits of the mitochondrial Nadh-ubiquinone-oxidoreductase (complex I). The carboxy-terminal end of the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/studies-on-the-expression-of-ndh-h-a-subunit-of-the-nadph-plastoquinone-oxidoreductase-of-higher-plant-chloroplasts/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on substances with sex pheromone activity produced by Heterodera schachtii females</title><link>http://scien.net/enzyme/peptide/studies-on-substances-with-sex-pheromone-activity-produced-by-heterodera-schachtii-females</link> <comments>http://scien.net/enzyme/peptide/studies-on-substances-with-sex-pheromone-activity-produced-by-heterodera-schachtii-females#comments</comments> <pubDate>Sat, 11 May 2013 06:02:19 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Peptide]]></category> <category><![CDATA[attractivity]]></category> <category><![CDATA[biotest]]></category> <category><![CDATA[vanillic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/peptide/studies-on-substances-with-sex-pheromone-activity-produced-by-heterodera-schachtii-females</guid> <description><![CDATA[Aumann, Jens; Hashem, Mohamed, 1993: Studies on substances with sex pheromone activity produced by Heterodera schachtii females. Fundamental &#038; Applied Nematology. 16(1): 43-46 Extracts from white, living, intact females of Heterodera schachtii were prepared with either n-hexane, ethyl acetate, methylene chloride, methanol, or water. All extracts showed sex pheromone activity for males in a biotest [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/peptide/studies-on-substances-with-sex-pheromone-activity-produced-by-heterodera-schachtii-females/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on ocular microsporidia</title><link>http://scien.net/enzyme/immunosorbent/studies-on-ocular-microsporidia</link> <comments>http://scien.net/enzyme/immunosorbent/studies-on-ocular-microsporidia#comments</comments> <pubDate>Sat, 11 May 2013 06:01:58 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Immunosorbent]]></category> <category><![CDATA[algerae]]></category> <category><![CDATA[cuniculi]]></category> <category><![CDATA[encephalitozoon]]></category> <category><![CDATA[hellem]]></category> <category><![CDATA[microsporidial]]></category> <category><![CDATA[microsporidiosis]]></category><guid
isPermaLink="false">http://scien.net/enzyme/immunosorbent/studies-on-ocular-microsporidia</guid> <description><![CDATA[Didier E.S.; Shadduck J.A.; Didier P.J.; Millichamp N.; Vossbrinck C.R., 1991: Studies on ocular microsporidia. Journal Of Protozoology. 38(6): 635-638 Sera from six ocular microsporidiosis patients and eight individuals with no history of microsporidiosis were assayed by enzyme-linked immunosorbent assay (Elisa) and by Western blot immunodetection. Microsporidia used as antigen include Nosema corneum, Encephalitozoon hellem, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/immunosorbent/studies-on-ocular-microsporidia/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on mitochondrial ATPase of Leishmania donovani using digitonin-permeabilized promastigotes</title><link>http://scien.net/enzyme/studies-on-mitochondrial-atpase-of-leishmania-donovani-using-digitonin-permeabilized-promastigotes</link> <comments>http://scien.net/enzyme/studies-on-mitochondrial-atpase-of-leishmania-donovani-using-digitonin-permeabilized-promastigotes#comments</comments> <pubDate>Sat, 11 May 2013 06:01:51 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[dccd]]></category> <category><![CDATA[hexanol]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studies-on-mitochondrial-atpase-of-leishmania-donovani-using-digitonin-permeabilized-promastigotes</guid> <description><![CDATA[Das, Amaresh, 1993: Studies on mitochondrial ATPase of Leishmania donovani using digitonin-permeabilized promastigotes. Molecular &#038; Biochemical Parasitology. 60(2): 293-301 Mitochondrial ATPase of Leishmania donovani was characterized using digitonin-permeabilized promastigotes and the results were compared with those from isolated mitochondria. Maximum mitochondrial ATPase activity was obtained in promastigotes permeabilized with digitonin at a final concentration of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studies-on-mitochondrial-atpase-of-leishmania-donovani-using-digitonin-permeabilized-promastigotes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on how phytoseiid mites feed on spider mites and pollen</title><link>http://scien.net/enzyme/studies-on-how-phytoseiid-mites-feed-on-spider-mites-and-pollen</link> <comments>http://scien.net/enzyme/studies-on-how-phytoseiid-mites-feed-on-spider-mites-and-pollen#comments</comments> <pubDate>Sat, 11 May 2013 06:01:40 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[chelicerae]]></category> <category><![CDATA[cheliceral]]></category> <category><![CDATA[degenerans]]></category> <category><![CDATA[euseius]]></category> <category><![CDATA[galendromus]]></category> <category><![CDATA[iphiseius]]></category> <category><![CDATA[phytoseiulus]]></category> <category><![CDATA[preoral]]></category> <category><![CDATA[similoides]]></category> <category><![CDATA[stipulatus]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studies-on-how-phytoseiid-mites-feed-on-spider-mites-and-pollen</guid> <description><![CDATA[Flechtmann C.H.W.; Mcmurtry J.A., 1992: Studies on how phytoseiid mites feed on spider mites and pollen. International Journal Of Acarology. 18(3): 157-162 Galendromus occidentalis, Phytoseiulus fragariae, Euseius stipulatus, Amblyseius similoides and Iphiseius degenerans feed on spider mites by cutting into the cuticle of the prey with their chelicerae; the cornuculi are partially introduced after cheliceral [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studies-on-how-phytoseiid-mites-feed-on-spider-mites-and-pollen/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies on experimental chlamydial mastitis in goat histoenzymology</title><link>http://scien.net/enzyme/dehydrogenase/studies-on-experimental-chlamydial-mastitis-in-goat-histoenzymology</link> <comments>http://scien.net/enzyme/dehydrogenase/studies-on-experimental-chlamydial-mastitis-in-goat-histoenzymology#comments</comments> <pubDate>Sat, 11 May 2013 06:01:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[acpase]]></category> <category><![CDATA[akpase]]></category> <category><![CDATA[histoenzymic]]></category> <category><![CDATA[histoenzymology]]></category> <category><![CDATA[intracisternally]]></category> <category><![CDATA[perilobular]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/studies-on-experimental-chlamydial-mastitis-in-goat-histoenzymology</guid> <description><![CDATA[Koul, Suman; Singh, Jaswant; Dhingra, P. N.; Khatra, G. S., 1993: Studies on experimental chlamydial mastitis in goat histoenzymology. Comparative Immunology Microbiology &#038; Infectious Diseases. 16(4): 307-316 Two strains of Chlamydia psittaci (one isolated from aborted goat foetus and the other from brain of a buffalo calf that had died of meningoencephalitis) were injected intracisternally [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/studies-on-experimental-chlamydial-mastitis-in-goat-histoenzymology/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies of the enzymic capacities and transport properties of pea root plastids</title><link>http://scien.net/enzyme/dehydrogenase/studies-of-the-enzymic-capacities-and-transport-properties-of-pea-root-plastids</link> <comments>http://scien.net/enzyme/dehydrogenase/studies-of-the-enzymic-capacities-and-transport-properties-of-pea-root-plastids#comments</comments> <pubDate>Sat, 11 May 2013 06:00:43 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[counterexchange]]></category> <category><![CDATA[dhap]]></category> <category><![CDATA[intactness]]></category> <category><![CDATA[phosphoglyceromutase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/studies-of-the-enzymic-capacities-and-transport-properties-of-pea-root-plastids</guid> <description><![CDATA[Borchert, S; Harborth, J; Schunemann, D; Hoferichter, P; Heldt, Hw, 1993: Studies of the enzymic capacities and transport properties of pea root plastids. Plant physiology 101(1): 303-312 Plastids have been isolated from pea (Pisum sativum L.) roots with a high degree of purity and intactness. In these plastids, the activity of enzymes involved in carbohydrate [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/studies-of-the-enzymic-capacities-and-transport-properties-of-pea-root-plastids/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Studies of aroma constituents bound as glycosides in tomato</title><link>http://scien.net/enzyme/studies-of-aroma-constituents-bound-as-glycosides-in-tomato</link> <comments>http://scien.net/enzyme/studies-of-aroma-constituents-bound-as-glycosides-in-tomato#comments</comments> <pubDate>Sat, 11 May 2013 06:00:35 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[glycosidically]]></category> <category><![CDATA[norisoprenoids]]></category> <category><![CDATA[phenylethanol]]></category> <category><![CDATA[shikimate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/studies-of-aroma-constituents-bound-as-glycosides-in-tomato</guid> <description><![CDATA[Marlatt C.; Ho C T.; Chien M., 1992: Studies of aroma constituents bound as glycosides in tomato. Journal Of Agricultural &#038; Food Chemistry. 40(2): 249-252 Glycosidically bound volatiles in fresh tomato have been studied. The glycosides were isolated from an aqueous extract of tomatoes by adsorption onto a column of Amberlite Xad-2, followed by washing [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/studies-of-aroma-constituents-bound-as-glycosides-in-tomato/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al</title><link>http://scien.net/enzyme/reductase/structures-of-genes-nasa-and-nasb-encoding-assimilatory-nitrate-and-nitrite-reductases-in-klebsiella-pneumoniae-m5al</link> <comments>http://scien.net/enzyme/reductase/structures-of-genes-nasa-and-nasb-encoding-assimilatory-nitrate-and-nitrite-reductases-in-klebsiella-pneumoniae-m5al#comments</comments> <pubDate>Sat, 11 May 2013 06:00:17 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Reductase]]></category> <category><![CDATA[molybdoenzymes]]></category> <category><![CDATA[narghj]]></category> <category><![CDATA[narghji]]></category> <category><![CDATA[narl]]></category> <category><![CDATA[nasb]]></category> <category><![CDATA[nasba]]></category><guid
isPermaLink="false">http://scien.net/enzyme/reductase/structures-of-genes-nasa-and-nasb-encoding-assimilatory-nitrate-and-nitrite-reductases-in-klebsiella-pneumoniae-m5al</guid> <description><![CDATA[Lin, Janine T.; Goldman, Barry S.; Stewart, Valley, 1993: Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al. Journal Of Bacteriology. 175(8): 2370-2378 Klebsiella pneumoniae can use nitrate and nitrite as sole nitrogen sources during aerobic growth. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/reductase/structures-of-genes-nasa-and-nasb-encoding-assimilatory-nitrate-and-nitrite-reductases-in-klebsiella-pneumoniae-m5al/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure-fungicidal properties of some 3- and 4-hydroxylated stilbenes and bibenzyl analogues</title><link>http://scien.net/enzyme/structure-fungicidal-properties-of-some-3-and-4-hydroxylated-stilbenes-and-bibenzyl-analogues</link> <comments>http://scien.net/enzyme/structure-fungicidal-properties-of-some-3-and-4-hydroxylated-stilbenes-and-bibenzyl-analogues#comments</comments> <pubDate>Sat, 11 May 2013 06:00:09 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[bibenzyl]]></category> <category><![CDATA[bibenzyls]]></category> <category><![CDATA[coriolus]]></category> <category><![CDATA[gloeophyllum]]></category> <category><![CDATA[hydroxybibenzyl]]></category> <category><![CDATA[hydroxystilbene]]></category> <category><![CDATA[pinosylvin]]></category> <category><![CDATA[poria]]></category> <category><![CDATA[stilbenes]]></category> <category><![CDATA[trabeum]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structure-fungicidal-properties-of-some-3-and-4-hydroxylated-stilbenes-and-bibenzyl-analogues</guid> <description><![CDATA[Schultz, Tp; Boldin, Wd; Fisher, Th; Nicholas, Dd; Mcmurtrey, Kd; Pobanz, K., 1992: Structure-fungicidal properties of some 3- and 4-hydroxylated stilbenes and bibenzyl analogues. Phytochemistry 31(11): 3801-3806 The fungicidal activity of some substituted hydroxylated stilbenes and bibenzyls was measured against three wood-destroying fungi using the agar plate technique. Four 3-hydroxystilbene derivatives and 3-hydroxybibenzyl were active [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structure-fungicidal-properties-of-some-3-and-4-hydroxylated-stilbenes-and-bibenzyl-analogues/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure-based inhibitor design by using protein models for the development of antiparasitic agents</title><link>http://scien.net/enzyme/structure-based-inhibitor-design-by-using-protein-models-for-the-development-of-antiparasitic-agents</link> <comments>http://scien.net/enzyme/structure-based-inhibitor-design-by-using-protein-models-for-the-development-of-antiparasitic-agents#comments</comments> <pubDate>Sat, 11 May 2013 06:00:09 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[methoxybenzoyl]]></category> <category><![CDATA[naphthoic]]></category> <category><![CDATA[nonpeptidic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structure-based-inhibitor-design-by-using-protein-models-for-the-development-of-antiparasitic-agents</guid> <description><![CDATA[Ring, Christine S.; Sun, Eugene; Mckerrow, James H.; Lee, Garson K.; Rosenthal, Philip J.; Kuntz, Irwin D.; Cohen, Fred E., 1993: Structure-based inhibitor design by using protein models for the development of antiparasitic agents. Proceedings Of The National Academy Of Sciences Of The United States Of America. 90(8): 3583-3587 The lack of an experimentally determined [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structure-based-inhibitor-design-by-using-protein-models-for-the-development-of-antiparasitic-agents/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure of the gene for the testis-specific proprotein convertase 4 and of its alternate messenger RNA isoforms</title><link>http://scien.net/enzyme/structure-of-the-gene-for-the-testis-specific-proprotein-convertase-4-and-of-its-alternate-messenger-rna-isoforms</link> <comments>http://scien.net/enzyme/structure-of-the-gene-for-the-testis-specific-proprotein-convertase-4-and-of-its-alternate-messenger-rna-isoforms#comments</comments> <pubDate>Sat, 11 May 2013 05:59:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[chretien]]></category> <category><![CDATA[collard]]></category> <category><![CDATA[convertases]]></category> <category><![CDATA[endocrinol]]></category> <category><![CDATA[endoproteinase]]></category> <category><![CDATA[furin]]></category> <category><![CDATA[gaspar]]></category> <category><![CDATA[gggcgg]]></category> <category><![CDATA[hamelin]]></category> <category><![CDATA[nonsecretory]]></category> <category><![CDATA[proprotein]]></category> <category><![CDATA[tataa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structure-of-the-gene-for-the-testis-specific-proprotein-convertase-4-and-of-its-alternate-messenger-rna-isoforms</guid> <description><![CDATA[Mbikay, Majambu; Raffin Sanson, Marie Laure; Tadros, Haidy; Sirois, Francine; Seidah, Nabil G.; Chretien, Michel, 1994: Structure of the gene for the testis-specific proprotein convertase 4 and of its alternate messenger RNA isoforms. Genomics. 20(2): 231-237 Proprotein convertase 4 (Pc4) is a mammalian secretory serine endoproteinase similar to the yeast Kex2 gene product and specifically [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structure-of-the-gene-for-the-testis-specific-proprotein-convertase-4-and-of-its-alternate-messenger-rna-isoforms/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data</title><link>http://scien.net/enzyme/dehydrogenase/structure-of-glycosomal-glyceraldehyde-3-phosphate-dehydrogenase-from-trypanosoma-brucei-determined-from-laue-data</link> <comments>http://scien.net/enzyme/dehydrogenase/structure-of-glycosomal-glyceraldehyde-3-phosphate-dehydrogenase-from-trypanosoma-brucei-determined-from-laue-data#comments</comments> <pubDate>Sat, 11 May 2013 05:59:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[glycosomal]]></category> <category><![CDATA[laue]]></category> <category><![CDATA[phosphatenad]]></category> <category><![CDATA[polychromatic]]></category> <category><![CDATA[skarzynski]]></category> <category><![CDATA[wonacott]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/structure-of-glycosomal-glyceraldehyde-3-phosphate-dehydrogenase-from-trypanosoma-brucei-determined-from-laue-data</guid> <description><![CDATA[Vellieux, Fred M. D.; Hajdu, Janos; Verlinde, Christophe L. M. J.; Groendijk, Hillie; Read, Randy J.; Greenhough, Trevor J.; Campbell, John W.; Kalik, Kor H.; Littlechild, Jenny A., 1993: Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data. Proceedings Of The National Academy Of Sciences Of The United States Of America. 90(6): [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/structure-of-glycosomal-glyceraldehyde-3-phosphate-dehydrogenase-from-trypanosoma-brucei-determined-from-laue-data/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure and organization of mouse GlcNAc-1-phosphate transferase gene</title><link>http://scien.net/enzyme/polymerase/structure-and-organization-of-mouse-glcnac-1-phosphate-transferase-gene</link> <comments>http://scien.net/enzyme/polymerase/structure-and-organization-of-mouse-glcnac-1-phosphate-transferase-gene#comments</comments> <pubDate>Sat, 11 May 2013 05:58:41 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Polymerase]]></category> <category><![CDATA[dolichol]]></category> <category><![CDATA[exonintron]]></category> <category><![CDATA[glcnacdolichol]]></category><guid
isPermaLink="false">http://scien.net/enzyme/polymerase/structure-and-organization-of-mouse-glcnac-1-phosphate-transferase-gene</guid> <description><![CDATA[Rajput, Bhanu; Ma, Jie; Vijay, Inder K., 1994: Structure and organization of mouse GlcNAc-1-phosphate transferase gene. Journal Of Biological Chemistry. 269(13): 9590-9597 The gene encoding Udp-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase (Gpt), the enzyme that initiates the pathway for the biosynthesis of asparagine-linked glycoproteins, was isolated and characterized. Southern blot analyses demonstrated a single copy gene for [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/polymerase/structure-and-organization-of-mouse-glcnac-1-phosphate-transferase-gene/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction</title><link>http://scien.net/enzyme/polymerase/structure-and-expression-of-chloroplast-localized-porphobilinogen-deaminase-from-pea-pisum-sativum-l-isolated-by-redundant-polymerase-chain-reaction</link> <comments>http://scien.net/enzyme/polymerase/structure-and-expression-of-chloroplast-localized-porphobilinogen-deaminase-from-pea-pisum-sativum-l-isolated-by-redundant-polymerase-chain-reaction#comments</comments> <pubDate>Sat, 11 May 2013 05:58:14 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Polymerase]]></category> <category><![CDATA[deaminases]]></category> <category><![CDATA[hydroxymethylbilane]]></category> <category><![CDATA[monopyrrole]]></category> <category><![CDATA[porphobilinogen]]></category> <category><![CDATA[taqi]]></category> <category><![CDATA[tetrapyrrole]]></category><guid
isPermaLink="false">http://scien.net/enzyme/polymerase/structure-and-expression-of-chloroplast-localized-porphobilinogen-deaminase-from-pea-pisum-sativum-l-isolated-by-redundant-polymerase-chain-reaction</guid> <description><![CDATA[Witty, M.; Wallace Cook, A. D. M.; Albrecht, H.; Spano, A. J.; Michel, H.; Shabanowitz, J.; Hunt, D. F.; Timko, M. P.; Smith, A. G., 1993: Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction. Plant Physiology 103(1): 139-147 Porphobilinogen (Pbg) deaminase catalyzes the polymerization of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/polymerase/structure-and-expression-of-chloroplast-localized-porphobilinogen-deaminase-from-pea-pisum-sativum-l-isolated-by-redundant-polymerase-chain-reaction/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structure and expression of a sugarcane gene encoding a housekeeping phosphoenolpyruvate carboxylase</title><link>http://scien.net/enzyme/structure-and-expression-of-a-sugarcane-gene-encoding-a-housekeeping-phosphoenolpyruvate-carboxylase</link> <comments>http://scien.net/enzyme/structure-and-expression-of-a-sugarcane-gene-encoding-a-housekeeping-phosphoenolpyruvate-carboxylase#comments</comments> <pubDate>Sat, 11 May 2013 05:58:09 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[pepc]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structure-and-expression-of-a-sugarcane-gene-encoding-a-housekeeping-phosphoenolpyruvate-carboxylase</guid> <description><![CDATA[Albert, Ha; Martin, T; Sun, Ssm, 1992: Structure and expression of a sugarcane gene encoding a housekeeping phosphoenolpyruvate carboxylase. Plant molecular biology: an international journal on molecular biology biochemistry and genetic engineering 20(4): 663-671 A gene (Scpepcd1) encoding phosphoenolpyruvate carboxylase (Pepc) was isolated from the C-4 monocot sugarcane (Saccharum hybrid var. H32-8560). Scpepcd1 is ca. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structure-and-expression-of-a-sugarcane-gene-encoding-a-housekeeping-phosphoenolpyruvate-carboxylase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structural organization of the components of the cell wall from Candida albicans</title><link>http://scien.net/enzyme/structural-organization-of-the-components-of-the-cell-wall-from-candida-albicans</link> <comments>http://scien.net/enzyme/structural-organization-of-the-components-of-the-cell-wall-from-candida-albicans#comments</comments> <pubDate>Sat, 11 May 2013 05:57:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[mannoproteins]]></category> <category><![CDATA[zymolyase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structural-organization-of-the-components-of-the-cell-wall-from-candida-albicans</guid> <description><![CDATA[Ruiz Herrera, Jose; Mormeneo, Salvador; Vanaclocha, Pilar; Font De Mora, Jaime; Iranzo, Maria; Puertes, Inmaculada; Sentandreu, Rafael, 1994: Structural organization of the components of the cell wall from Candida albicans. Microbiology (reading). 140(7): 1513-1523 The organization of the components of the cell wall from Candida albicans was studied by means of sequential treatment with hot [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structural-organization-of-the-components-of-the-cell-wall-from-candida-albicans/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structural organization of de novo purine biosynthesis enzymes in plants: 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase cDNAs from Vigna aconitifolia</title><link>http://scien.net/enzyme/escherichia/structural-organization-of-de-novo-purine-biosynthesis-enzymes-in-plants-5-aminoimidazole-ribonucleotide-carboxylase-and-5-aminoimidazole-4-n-succinocarboxamide-ribonucleotide-synthetase-cdnas-from-v</link> <comments>http://scien.net/enzyme/escherichia/structural-organization-of-de-novo-purine-biosynthesis-enzymes-in-plants-5-aminoimidazole-ribonucleotide-carboxylase-and-5-aminoimidazole-4-n-succinocarboxamide-ribonucleotide-synthetase-cdnas-from-v#comments</comments> <pubDate>Sat, 11 May 2013 05:57:21 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[aconitifolia]]></category> <category><![CDATA[aminoimidazole]]></category> <category><![CDATA[mothbean]]></category> <category><![CDATA[purc]]></category> <category><![CDATA[purk]]></category> <category><![CDATA[saicar]]></category> <category><![CDATA[succinocarboxamide]]></category> <category><![CDATA[ureides]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/structural-organization-of-de-novo-purine-biosynthesis-enzymes-in-plants-5-aminoimidazole-ribonucleotide-carboxylase-and-5-aminoimidazole-4-n-succinocarboxamide-ribonucleotide-synthetase-cdnas-from-v</guid> <description><![CDATA[Chapman, K. A.; Delauney, A. J.; Kim, J. H.; Verma, D. P. S., 1994: Structural organization of de novo purine biosynthesis enzymes in plants: 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase cDNAs from Vigna aconitifolia. Plant Molecular Biology 24(2): 389-395 Nodules of tropical legumes generally export symbiotically fixed nitrogen in the form of ureides that [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/structural-organization-of-de-novo-purine-biosynthesis-enzymes-in-plants-5-aminoimidazole-ribonucleotide-carboxylase-and-5-aminoimidazole-4-n-succinocarboxamide-ribonucleotide-synthetase-cdnas-from-v/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structural analysis of two length variants of the rDNA intergenic spacer from Eruca sativa</title><link>http://scien.net/enzyme/structural-analysis-of-two-length-variants-of-the-rdna-intergenic-spacer-from-eruca-sativa</link> <comments>http://scien.net/enzyme/structural-analysis-of-two-length-variants-of-the-rdna-intergenic-spacer-from-eruca-sativa#comments</comments> <pubDate>Sat, 11 May 2013 05:56:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[eruca]]></category> <category><![CDATA[itsa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/structural-analysis-of-two-length-variants-of-the-rdna-intergenic-spacer-from-eruca-sativa</guid> <description><![CDATA[Laksmikumaran, M; Negi, Ms, 1994: Structural analysis of two length variants of the rDNA intergenic spacer from Eruca sativa. Plant molecular biology 24(6): 915-927 Restriction enzyme analysis of the rRNA genes of Eruca sativa indicated the presence of many length variants within a single plant and also between different cultivars which is unusual for most [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/structural-analysis-of-two-length-variants-of-the-rdna-intergenic-spacer-from-eruca-sativa/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Structural analysis of the light subunit of the Entamoeba histolytica galactose-specific adherence lectin</title><link>http://scien.net/enzyme/peptide/structural-analysis-of-the-light-subunit-of-the-entamoeba-histolytica-galactose-specific-adherence-lectin</link> <comments>http://scien.net/enzyme/peptide/structural-analysis-of-the-light-subunit-of-the-entamoeba-histolytica-galactose-specific-adherence-lectin#comments</comments> <pubDate>Sat, 11 May 2013 05:56:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Peptide]]></category> <category><![CDATA[amebiasis]]></category> <category><![CDATA[chiro]]></category> <category><![CDATA[inositols]]></category><guid
isPermaLink="false">http://scien.net/enzyme/peptide/structural-analysis-of-the-light-subunit-of-the-entamoeba-histolytica-galactose-specific-adherence-lectin</guid> <description><![CDATA[Mccoy, James J.; Mann, Barbara J.; Vedvick, Thomas S.; Pak, Yunbae; Heimark, Douglas B.; Petri, Willaim A.Jr, 1993: Structural analysis of the light subunit of the Entamoeba histolytica galactose-specific adherence lectin. Journal Of Biological Chemistry. 268(32): 24223-24231 Adherence of Entamoeba histolytica trophozoites to colonic mucins and resistance to lysis by the membrane attack complex of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/peptide/structural-analysis-of-the-light-subunit-of-the-entamoeba-histolytica-galactose-specific-adherence-lectin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Strip ELISA for detection of staphylococcal enterotoxins in culture supernatants and foods</title><link>http://scien.net/enzyme/peroxidase/strip-elisa-for-detection-of-staphylococcal-enterotoxins-in-culture-supernatants-and-foods</link> <comments>http://scien.net/enzyme/peroxidase/strip-elisa-for-detection-of-staphylococcal-enterotoxins-in-culture-supernatants-and-foods#comments</comments> <pubDate>Sat, 11 May 2013 05:56:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Peroxidase]]></category> <category><![CDATA[noodles]]></category> <category><![CDATA[tetramethylbenzidine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/peroxidase/strip-elisa-for-detection-of-staphylococcal-enterotoxins-in-culture-supernatants-and-foods</guid> <description><![CDATA[Jung, Roland; Terplan, Gerhard, 1993: Strip ELISA for detection of staphylococcal enterotoxins in culture supernatants and foods. Food &#038; Agricultural Immunology. 5(2): 107-114 For the easy and rapid detection of staphylococcal enterotoxins (Se) A, B, C-1, D and E, a sandwich Elisa (enzyme-linked immunosorbent assay) was developed using an activated nylon membrane with covalently bound [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/peroxidase/strip-elisa-for-detection-of-staphylococcal-enterotoxins-in-culture-supernatants-and-foods/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis</title><link>http://scien.net/enzyme/strictosidine-synthase-from-rauvolfia-serpentina-analysis-of-a-gene-involved-in-indole-alkaloid-biosynthesis</link> <comments>http://scien.net/enzyme/strictosidine-synthase-from-rauvolfia-serpentina-analysis-of-a-gene-involved-in-indole-alkaloid-biosynthesis#comments</comments> <pubDate>Sat, 11 May 2013 05:56:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[mannii]]></category> <category><![CDATA[plumbaginifolia]]></category> <category><![CDATA[rauvolfia]]></category> <category><![CDATA[secologanin]]></category> <category><![CDATA[serpentina]]></category> <category><![CDATA[strictosidine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/strictosidine-synthase-from-rauvolfia-serpentina-analysis-of-a-gene-involved-in-indole-alkaloid-biosynthesis</guid> <description><![CDATA[Bracher, D.; Kutchan, T. M., 1992: Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis. Archives of Biochemistry and Biophysics 294(2): 717-723 The gene for strictosidine synthase (str1), the enzyme which catalyzes the stereospecific condensation of tryptamine and secologanin to form the key indole alkaloid 3 alpha(S)-strictosidine has been isolated [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/strictosidine-synthase-from-rauvolfia-serpentina-analysis-of-a-gene-involved-in-indole-alkaloid-biosynthesis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Stress proteins in plants</title><link>http://scien.net/enzyme/stress-proteins-in-plants</link> <comments>http://scien.net/enzyme/stress-proteins-in-plants#comments</comments> <pubDate>Sat, 11 May 2013 05:56:06 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category><guid
isPermaLink="false">http://scien.net/enzyme/stress-proteins-in-plants</guid> <description><![CDATA[Burdon, Roy H., 1993: Stress proteins in plants. Botanical Journal Of Scotland. 46(3): 463-475 Several environmental stresses elicit specific plant genomic responses. These include temperature extremes, oxidative stress, water stress, anaerobiosis as well as pathogen attack. Molecular biological approaches are now yielding insights into the mechanisms whereby plant cells perceive the stress of temperature extremes [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/stress-proteins-in-plants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions</title><link>http://scien.net/enzyme/strength-of-protein-gels-prepared-with-microbial-transglutaminase-as-related-to-reaction-conditions</link> <comments>http://scien.net/enzyme/strength-of-protein-gels-prepared-with-microbial-transglutaminase-as-related-to-reaction-conditions#comments</comments> <pubDate>Sat, 11 May 2013 05:55:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Enzyme]]></category> <category><![CDATA[glutamyllysine]]></category> <category><![CDATA[tgase]]></category> <category><![CDATA[unitsg]]></category><guid
isPermaLink="false">http://scien.net/enzyme/strength-of-protein-gels-prepared-with-microbial-transglutaminase-as-related-to-reaction-conditions</guid> <description><![CDATA[Sakamoto, H; Kumazawa, Y; Motoki, M., 1994: Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. Journal of food science 59(4): 866-871 Influence of gelling reaction conditions on the strength of several protein gels prepared with microbial transglutaminase (TGase) was investigated. A method was developed to gel proteins and measure gel [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/strength-of-protein-gels-prepared-with-microbial-transglutaminase-as-related-to-reaction-conditions/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Strain-specific monoclonal antibodies to Penicillium bilaii</title><link>http://scien.net/enzyme/immunosorbent/strain-specific-monoclonal-antibodies-to-penicillium-bilaii</link> <comments>http://scien.net/enzyme/immunosorbent/strain-specific-monoclonal-antibodies-to-penicillium-bilaii#comments</comments> <pubDate>Sat, 11 May 2013 05:55:20 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Immunosorbent]]></category> <category><![CDATA[bilaii]]></category> <category><![CDATA[crustosum]]></category> <category><![CDATA[implicatum]]></category> <category><![CDATA[lapidosum]]></category><guid
isPermaLink="false">http://scien.net/enzyme/immunosorbent/strain-specific-monoclonal-antibodies-to-penicillium-bilaii</guid> <description><![CDATA[Zawistowski, J.; Gosek, L.; Cunningham, J. E., 1993: Strain-specific monoclonal antibodies to Penicillium bilaii. Food &#038; Agricultural Immunology. 5(4): 241-254 Monoclonal antibodies (IgM class) to Penicillium bilaii (isolate Pb-50) were developed and their specificity was determined against various fungi using enzyme-linked immunosorbent assays. Cross-reactivity in the range 0-6.5% was obtained for Fusarium, Aspergillus, Paecilomyces and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/immunosorbent/strain-specific-monoclonal-antibodies-to-penicillium-bilaii/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>
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