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><channel><title>Natural Sciences Bibliography &#187; Oxidase</title> <atom:link href="http://scien.net/category/enzyme/oxidase/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>205,000 References and 140,000 Tags</description> <lastBuildDate>Tue, 21 May 2013 03:34:42 +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>Relationship between apple ripening and browning: changes in polyphenol content and polyphenol oxidase</title><link>http://scien.net/enzyme/oxidase/relationship-between-apple-ripening-and-browning-changes-in-polyphenol-content-and-polyphenol-oxidase</link> <comments>http://scien.net/enzyme/oxidase/relationship-between-apple-ripening-and-browning-changes-in-polyphenol-content-and-polyphenol-oxidase#comments</comments> <pubDate>Tue, 21 May 2013 03:21:21 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/relationship-between-apple-ripening-and-browning-changes-in-polyphenol-content-and-polyphenol-oxidase</guid> <description><![CDATA[Murata, M.; Tsurutani, M.; Tomita, M.; Homma, S.; Kaneko, K., 1995: Relationship between apple ripening and browning: changes in polyphenol content and polyphenol oxidase. Journal of Agricultural and Food Chemistry 43(5): 1115-1121 Changes in the browning of apple juice, polyphenol content, and polyphenol oxidase were examined during apple ripening. The degree of browning of apple [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/relationship-between-apple-ripening-and-browning-changes-in-polyphenol-content-and-polyphenol-oxidase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Regulation of alternative oxidase activity by pyruvate in soybean mitochondria</title><link>http://scien.net/enzyme/oxidase/regulation-of-alternative-oxidase-activity-by-pyruvate-in-soybean-mitochondria</link> <comments>http://scien.net/enzyme/oxidase/regulation-of-alternative-oxidase-activity-by-pyruvate-in-soybean-mitochondria#comments</comments> <pubDate>Tue, 21 May 2013 03:17:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[intramitochondrial]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/regulation-of-alternative-oxidase-activity-by-pyruvate-in-soybean-mitochondria</guid> <description><![CDATA[Day, Da; Millar, Ah; Wiskich, Jt; Whelan, J., 1994: Regulation of alternative oxidase activity by pyruvate in soybean mitochondria. Plant physiology 106(4): 1421-1427 The regulation of alternative oxidase activity by the effector pyruvate was investigated in soybean (Glycine max L.) mitochondria using developmental changes in roots and cotyledons to vary the respiratory capacity of the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/regulation-of-alternative-oxidase-activity-by-pyruvate-in-soybean-mitochondria/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Pyruvate overflow and carbon flux within the central metabolic pathways of Corynebacterium glutamicum during growth on lactate</title><link>http://scien.net/enzyme/oxidase/pyruvate-overflow-and-carbon-flux-within-the-central-metabolic-pathways-of-corynebacterium-glutamicum-during-growth-on-lactate</link> <comments>http://scien.net/enzyme/oxidase/pyruvate-overflow-and-carbon-flux-within-the-central-metabolic-pathways-of-corynebacterium-glutamicum-during-growth-on-lactate#comments</comments> <pubDate>Tue, 21 May 2013 02:57:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[glutamicum]]></category> <category><![CDATA[nadhnadp]]></category> <category><![CDATA[overproduce]]></category> <category><![CDATA[transhydrogenase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/pyruvate-overflow-and-carbon-flux-within-the-central-metabolic-pathways-of-corynebacterium-glutamicum-during-growth-on-lactate</guid> <description><![CDATA[Cocaign Bousquet, Muriel; Lindley, Nicholas D., 1995: Pyruvate overflow and carbon flux within the central metabolic pathways of Corynebacterium glutamicum during growth on lactate. Enzyme &#038; Microbial Technology. 17(3): 260-267 Growth of Corynebacterium glutamicum was characterized kinetically for chemostat cultures using lactate as the sole carbon substrate, and the concentration profile of various enzymes of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/pyruvate-overflow-and-carbon-flux-within-the-central-metabolic-pathways-of-corynebacterium-glutamicum-during-growth-on-lactate/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification, characterization and developmental expression of indole-3-ethanol oxidase from seeds of Phaseolus vulgaris</title><link>http://scien.net/enzyme/oxidase/purification-characterization-and-developmental-expression-of-indole-3-ethanol-oxidase-from-seeds-of-phaseolus-vulgaris</link> <comments>http://scien.net/enzyme/oxidase/purification-characterization-and-developmental-expression-of-indole-3-ethanol-oxidase-from-seeds-of-phaseolus-vulgaris#comments</comments> <pubDate>Tue, 21 May 2013 02:56:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[indoleacetaldehyde]]></category> <category><![CDATA[induded]]></category> <category><![CDATA[losa]]></category> <category><![CDATA[tendergreen]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/purification-characterization-and-developmental-expression-of-indole-3-ethanol-oxidase-from-seeds-of-phaseolus-vulgaris</guid> <description><![CDATA[Zhu, Js; Scott, Gk, 1995: Purification, characterization and developmental expression of indole-3-ethanol oxidase from seeds of Phaseolus vulgaris. Biochemistry and molecular biology international 35(2): 423-432 Purification of indole-3-ethanol (IEt) oxidase was carried out from extracts of the seeds of two bean cultivars. The IEt oxidase from the Labrador cultivar was purified more than 1000 fold [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/purification-characterization-and-developmental-expression-of-indole-3-ethanol-oxidase-from-seeds-of-phaseolus-vulgaris/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and properties of the diamine oxidase of pea seedlings</title><link>http://scien.net/enzyme/oxidase/purification-and-properties-of-the-diamine-oxidase-of-pea-seedlings</link> <comments>http://scien.net/enzyme/oxidase/purification-and-properties-of-the-diamine-oxidase-of-pea-seedlings#comments</comments> <pubDate>Tue, 21 May 2013 02:56:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/purification-and-properties-of-the-diamine-oxidase-of-pea-seedlings</guid> <description><![CDATA[Deveci, Nuran; Guvenilir, Yuksel A., 1995: Purification and properties of the diamine oxidase of pea seedlings. Applied Biochemistry &#038; Biotechnology. 53(1): 83-90 Enzymes have been used extensively in many industries for the last 20 yrs. The purpose of this study was the isolation, purification, and specification of diamine oxidase (Dao) of pea seedlings. The relationship [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/purification-and-properties-of-the-diamine-oxidase-of-pea-seedlings/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of diamine oxidase from Zea mays shoots</title><link>http://scien.net/enzyme/oxidase/purification-and-characterization-of-diamine-oxidase-from-zea-mays-shoots</link> <comments>http://scien.net/enzyme/oxidase/purification-and-characterization-of-diamine-oxidase-from-zea-mays-shoots#comments</comments> <pubDate>Tue, 21 May 2013 02:55:29 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[quinoneimine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/purification-and-characterization-of-diamine-oxidase-from-zea-mays-shoots</guid> <description><![CDATA[Suzuki, Yonezo; Hagiwara, Masae, 1993: Purification and characterization of diamine oxidase from Zea mays shoots. Phytochemistry (oxford). 33(5): 995-998 Diamine oxidase (Dao) (Ec 1.4.3.6) activity was found in the shoots of seedlings of maize, oats, barley and wheat, using the quinoneimine reaction method. The enzyme was purified from maize shoots to apparent homogeneity using (Nh-4)-2so-4 [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/purification-and-characterization-of-diamine-oxidase-from-zea-mays-shoots/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit</title><link>http://scien.net/enzyme/oxidase/purification-and-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-apple-fruit</link> <comments>http://scien.net/enzyme/oxidase/purification-and-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-apple-fruit#comments</comments> <pubDate>Tue, 21 May 2013 02:55:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/purification-and-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-apple-fruit</guid> <description><![CDATA[Dong, Jg; Fernandez-Maculet, Jc; Yang, Sf, 1992: Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit. Proceedings of the National Academy of Sciences of the United States of America, 89(20): 9789-9793 1-aminocyclopropane-1-carboxylate (Acc) oxidase catalyzes the oxidation of Acc to ethylene. Following conventional column fractionation, the enzyme was purified 180-fold to near homogeneity with a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/purification-and-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-apple-fruit/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Purification and biochemical characterization of 1-aminocyclopropane-1-carboxylate oxidase from banana fruit</title><link>http://scien.net/enzyme/oxidase/purification-and-biochemical-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-banana-fruit</link> <comments>http://scien.net/enzyme/oxidase/purification-and-biochemical-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-banana-fruit#comments</comments> <pubDate>Tue, 21 May 2013 02:55:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[cavendish]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/purification-and-biochemical-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-banana-fruit</guid> <description><![CDATA[Moya Leon, Maria A.; John, Philip, 1995: Purification and biochemical characterization of 1-aminocyclopropane-1-carboxylate oxidase from banana fruit. Phytochemistry (oxford). 39(1): 15-20 A novel method using Peg and ammonium sulphate was used to concentrate Acc oxidase from a crude extract prepared from the pulp of ripe fruit of banana (Musa Aaa group, Cavendish subgroup). The 145-fold [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/purification-and-biochemical-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-from-banana-fruit/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Protoporphyrin accumulation induced by peroxidizing herbicides is counteracted by safeners</title><link>http://scien.net/enzyme/oxidase/protoporphyrin-accumulation-induced-by-peroxidizing-herbicides-is-counteracted-by-safeners</link> <comments>http://scien.net/enzyme/oxidase/protoporphyrin-accumulation-induced-by-peroxidizing-herbicides-is-counteracted-by-safeners#comments</comments> <pubDate>Tue, 21 May 2013 02:53:30 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[acifluorfen]]></category> <category><![CDATA[chlorophthalim]]></category> <category><![CDATA[dichloroacetyl]]></category> <category><![CDATA[imide]]></category> <category><![CDATA[methylester]]></category> <category><![CDATA[naphthalic]]></category> <category><![CDATA[nitrobenzoic]]></category> <category><![CDATA[peroxidizing]]></category> <category><![CDATA[protoporphyrinogen]]></category> <category><![CDATA[safener]]></category> <category><![CDATA[safeners]]></category> <category><![CDATA[safening]]></category> <category><![CDATA[tetrahydrophthalimide]]></category> <category><![CDATA[trifluoromethylphenox]]></category> <category><![CDATA[trimethylpyrrolo]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/protoporphyrin-accumulation-induced-by-peroxidizing-herbicides-is-counteracted-by-safeners</guid> <description><![CDATA[Boeger, Peter; Miller, Roswitha, 1994: Protoporphyrin accumulation induced by peroxidizing herbicides is counteracted by safeners. Zeitschrift Fuer Naturforschung Section C Biosciences. 49(11-12): 775-780 A number of safeners like naphthalene-1,8-dicarboxylic acid anhydride (naphthalic anhydride) or dichloroacetyl-hexahydro-3,3,8-alpha-trimethylpyrrolo-(1,2-alpha)-pyrimidine-6-(2h)-one (Bas 145138) drastically decreased the accumulation of protoporphyrin Ix induced by a peroxidative cyclic imide (chlorophthalim, N-(4-chlorophenyl)-3,4,5,6-tetrahydrophthalimide), or &#8211; ether [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/protoporphyrin-accumulation-induced-by-peroxidizing-herbicides-is-counteracted-by-safeners/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Protective effects of ginsenosides on oxygen free radical induced damages of cultured vascular endothelial cells in vitro</title><link>http://scien.net/enzyme/oxidase/protective-effects-of-ginsenosides-on-oxygen-free-radical-induced-damages-of-cultured-vascular-endothelial-cells-in-vitro</link> <comments>http://scien.net/enzyme/oxidase/protective-effects-of-ginsenosides-on-oxygen-free-radical-induced-damages-of-cultured-vascular-endothelial-cells-in-vitro#comments</comments> <pubDate>Tue, 21 May 2013 02:51:06 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[antiatherosclerosis]]></category> <category><![CDATA[electrolysis]]></category> <category><![CDATA[ginsenosides]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/protective-effects-of-ginsenosides-on-oxygen-free-radical-induced-damages-of-cultured-vascular-endothelial-cells-in-vitro</guid> <description><![CDATA[Mei, B.; Wang, Y. F.; Wu, J. X.; Chen, W. Z., 1994: Protective effects of ginsenosides on oxygen free radical induced damages of cultured vascular endothelial cells in vitro. Yaoxue Xuebao. 29(11): 801-808 In this study, calf aortic endothelial cells (Ecs) were cultured in vitro to study the ECs damages induced by exogenous oxygen free [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/protective-effects-of-ginsenosides-on-oxygen-free-radical-induced-damages-of-cultured-vascular-endothelial-cells-in-vitro/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Properties of carrot polyphenoloxidase</title><link>http://scien.net/enzyme/oxidase/properties-of-carrot-polyphenoloxidase</link> <comments>http://scien.net/enzyme/oxidase/properties-of-carrot-polyphenoloxidase#comments</comments> <pubDate>Tue, 21 May 2013 02:48:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[denaturating]]></category> <category><![CDATA[phenoloxidase]]></category> <category><![CDATA[polyphenoloxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/properties-of-carrot-polyphenoloxidase</guid> <description><![CDATA[Soderhall, Irene, 1995: Properties of carrot polyphenoloxidase. Phytochemistry (oxford). 39(1): 33-38 A latent phenoloxidase (Ppo) was purified in the presence of protease inhibitors from carrot cells to electrophoretic homogeneity. The inactive enzyme had a M-r of ca 59,000 under denaturating conditions as judged by Sds-Page. When stored in the absence of protease inhibitors, Ppo in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/properties-of-carrot-polyphenoloxidase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Properties of a long chain aldehyde-forming enzyme in the marine green alga Ulva pertusa</title><link>http://scien.net/enzyme/oxidase/properties-of-a-long-chain-aldehyde-forming-enzyme-in-the-marine-green-alga-ulva-pertusa</link> <comments>http://scien.net/enzyme/oxidase/properties-of-a-long-chain-aldehyde-forming-enzyme-in-the-marine-green-alga-ulva-pertusa#comments</comments> <pubDate>Tue, 21 May 2013 02:48:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[cellulofine]]></category> <category><![CDATA[pertusa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/properties-of-a-long-chain-aldehyde-forming-enzyme-in-the-marine-green-alga-ulva-pertusa</guid> <description><![CDATA[Kajiwara, Tadahiko; Hatanaka, Akikazu; Matsui, Kenji; Tomoi, Takashi; Idohara, Takeshi, 1994: Properties of a long chain aldehyde-forming enzyme in the marine green alga Ulva pertusa. Phytochemistry (oxford). 35(1): 55-57 A long chain aldehyde-forming enzyme (Lcae, alpha-oxidation enzyme) in the marine green alga, Ulva pertusa, was purified 53-fold by differential centrifugation and chromatography with a Deae [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/properties-of-a-long-chain-aldehyde-forming-enzyme-in-the-marine-green-alga-ulva-pertusa/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Preliminary characterization of 1-aminocyclopropane-1-carboxylate oxidase properties from embryonic axes of chick-pea (Cicer arietinum L.) seeds</title><link>http://scien.net/enzyme/oxidase/preliminary-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-properties-from-embryonic-axes-of-chick-pea-cicer-arietinum-l-seeds</link> <comments>http://scien.net/enzyme/oxidase/preliminary-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-properties-from-embryonic-axes-of-chick-pea-cicer-arietinum-l-seeds#comments</comments> <pubDate>Tue, 21 May 2013 02:34:21 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[acco]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/preliminary-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-properties-from-embryonic-axes-of-chick-pea-cicer-arietinum-l-seeds</guid> <description><![CDATA[Munoz de Rueda, P. M.; Gallardo, M.; Matilla, A. J.; Sanchez Calle, I. M., 1995: Preliminary characterization of 1-aminocyclopropane-1-carboxylate oxidase properties from embryonic axes of chick-pea (Cicer arietinum L.) seeds. Journal of Experimental Botany 46(287): 695-700 For a deeper understanding of the germination of chick-pea (Cicer arietinum) seeds, which is dependent upon ethylene synthesis, a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/preliminary-characterization-of-1-aminocyclopropane-1-carboxylate-oxidase-properties-from-embryonic-axes-of-chick-pea-cicer-arietinum-l-seeds/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Possible mechanism of diazinon negative cross-resistance in pyrethroid-resistant horn flies (Diptera: Muscidae)</title><link>http://scien.net/enzyme/oxidase/possible-mechanism-of-diazinon-negative-cross-resistance-in-pyrethroid-resistant-horn-flies-diptera-muscidae</link> <comments>http://scien.net/enzyme/oxidase/possible-mechanism-of-diazinon-negative-cross-resistance-in-pyrethroid-resistant-horn-flies-diptera-muscidae#comments</comments> <pubDate>Tue, 21 May 2013 02:25:27 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[diazoxon]]></category> <category><![CDATA[haematobia]]></category> <category><![CDATA[synergist]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/possible-mechanism-of-diazinon-negative-cross-resistance-in-pyrethroid-resistant-horn-flies-diptera-muscidae</guid> <description><![CDATA[Cilek, J. E.; Dahlman, D. L.; Knapp, F. W., 1995: Possible mechanism of diazinon negative cross-resistance in pyrethroid-resistant horn flies (Diptera: Muscidae). Journal of Economic Entomology 88(3): 520-524 The underlying mechanism responsible for enhanced toxicity of the organophosphate diazinon in eight pyrethroid-resistant horn fly, Haematobia irritans (L.), field populations was investigated. In vitro enzyme assays [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/possible-mechanism-of-diazinon-negative-cross-resistance-in-pyrethroid-resistant-horn-flies-diptera-muscidae/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Polyphenol oxidases produced by in vitro cultures of rosemary</title><link>http://scien.net/enzyme/oxidase/polyphenol-oxidases-produced-by-in-vitro-cultures-of-rosemary</link> <comments>http://scien.net/enzyme/oxidase/polyphenol-oxidases-produced-by-in-vitro-cultures-of-rosemary#comments</comments> <pubDate>Tue, 21 May 2013 02:21:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[rosemary]]></category> <category><![CDATA[rosmarinus]]></category> <category><![CDATA[superdex]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/polyphenol-oxidases-produced-by-in-vitro-cultures-of-rosemary</guid> <description><![CDATA[&#8220;Cai, Weiming S.; Martin, Richard; Lemaure, Bernard; Courtois, Didier; Petiard, Vincent, 1993: Polyphenol oxidases produced by in vitro cultures of rosemary. Plant Physiology &#038; Biochemistry (montrouge). 31(2): 233-240 Multiple polyphenol oxidase (Ppo) activities, excreted into the growing medium during the cell growth phase of rosemary (Rosmarinus officinalis) cell suspension cultures, have been separated by combinations [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/polyphenol-oxidases-produced-by-in-vitro-cultures-of-rosemary/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Polyamine metabolism and in vitro cell multiplication and differentiation in leaf explants of Chrysanthemum morifolium Ramat</title><link>http://scien.net/enzyme/oxidase/polyamine-metabolism-and-in-vitro-cell-multiplication-and-differentiation-in-leaf-explants-of-chrysanthemum-morifolium-ramat</link> <comments>http://scien.net/enzyme/oxidase/polyamine-metabolism-and-in-vitro-cell-multiplication-and-differentiation-in-leaf-explants-of-chrysanthemum-morifolium-ramat#comments</comments> <pubDate>Tue, 21 May 2013 02:19:39 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[dfmo]]></category> <category><![CDATA[difluoromethylomithine]]></category> <category><![CDATA[ethylhydrazine]]></category> <category><![CDATA[facilated]]></category> <category><![CDATA[indolylacetic]]></category> <category><![CDATA[morifolium]]></category> <category><![CDATA[oxydase]]></category> <category><![CDATA[ramat]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/polyamine-metabolism-and-in-vitro-cell-multiplication-and-differentiation-in-leaf-explants-of-chrysanthemum-morifolium-ramat</guid> <description><![CDATA[Aribaud, M; Carre, M; Martin-Tanguy, J., 1994: Polyamine metabolism and in vitro cell multiplication and differentiation in leaf explants of Chrysanthemum morifolium Ramat. Plant growth regulation 15(2): 143-155 Arginine decarboxylase (Adc), ornithine decarboxylase (Odc), diamine oxydase (Dao) free amine and conjugated amine titers were estimated in leaf explants of Chrysanthemum morifolium Ramat. var. Spinder cultivated [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/polyamine-metabolism-and-in-vitro-cell-multiplication-and-differentiation-in-leaf-explants-of-chrysanthemum-morifolium-ramat/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Plant cytotoxicity of nebularine (purine riboside)</title><link>http://scien.net/enzyme/oxidase/plant-cytotoxicity-of-nebularine-purine-riboside</link> <comments>http://scien.net/enzyme/oxidase/plant-cytotoxicity-of-nebularine-purine-riboside#comments</comments> <pubDate>Tue, 21 May 2013 02:12:18 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[clitocybe]]></category> <category><![CDATA[lepista]]></category> <category><![CDATA[nebularine]]></category> <category><![CDATA[nebularis]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/plant-cytotoxicity-of-nebularine-purine-riboside</guid> <description><![CDATA[Brown, E. G.; Konuk, M., 1994: Plant cytotoxicity of nebularine (purine riboside). Phytochemistry 37(6): 1589-1592 The plant cytotoxicity of nebularine, a purine riboside antibiotic produced by the fungus Lepista (Clitocybe) nebularis, has been examined. The compound inhibits the growth of seedlings of various species and causes mitotic aberrations in root tips. Because of the potent [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/plant-cytotoxicity-of-nebularine-purine-riboside/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Photosynthetic enzyme activities in Vetiveria zizanioides cultivated in temperate climates</title><link>http://scien.net/enzyme/oxidase/photosynthetic-enzyme-activities-in-vetiveria-zizanioides-cultivated-in-temperate-climates</link> <comments>http://scien.net/enzyme/oxidase/photosynthetic-enzyme-activities-in-vetiveria-zizanioides-cultivated-in-temperate-climates#comments</comments> <pubDate>Tue, 21 May 2013 02:05:36 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[graminaceous]]></category> <category><![CDATA[vetiver]]></category> <category><![CDATA[vetiveria]]></category> <category><![CDATA[zizanioides]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/photosynthetic-enzyme-activities-in-vetiveria-zizanioides-cultivated-in-temperate-climates</guid> <description><![CDATA[Maffei, M; Scannerini, S; Berta, G; Mucciarelli, M., 1995: Photosynthetic enzyme activities in Vetiveria zizanioides cultivated in temperate climates. Biochemical systematics and ecology 23(1): 27-32 Delta 13c values, Phosphoenolpyruvate carboxylase, ribulose-1,5-bisphosphate and glycolate-oxidase activities were determined in Vetiveria zizanioides Stapf. (Vetiver) a graminaceous plant native to tropical and subtropical areas. The results obtained allowed us [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/photosynthetic-enzyme-activities-in-vetiveria-zizanioides-cultivated-in-temperate-climates/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Peroxidizing phytotoxic activity of 1,3,4-thiadiazolidine-2-thiones and 1,2,4-triazolidine-3,5-dithiones</title><link>http://scien.net/enzyme/oxidase/peroxidizing-phytotoxic-activity-of-134-thiadiazolidine-2-thiones-and-124-triazolidine-35-dithiones</link> <comments>http://scien.net/enzyme/oxidase/peroxidizing-phytotoxic-activity-of-134-thiadiazolidine-2-thiones-and-124-triazolidine-35-dithiones#comments</comments> <pubDate>Tue, 21 May 2013 01:55:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[acutus]]></category> <category><![CDATA[arylimino]]></category> <category><![CDATA[dithiones]]></category> <category><![CDATA[imides]]></category> <category><![CDATA[peroxidizing]]></category> <category><![CDATA[protoporphyrinogen]]></category> <category><![CDATA[tetramethylene]]></category> <category><![CDATA[thiadiazolidine]]></category> <category><![CDATA[thiones]]></category> <category><![CDATA[triazolidine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/peroxidizing-phytotoxic-activity-of-134-thiadiazolidine-2-thiones-and-124-triazolidine-35-dithiones</guid> <description><![CDATA[Ihara, Tetsushi; IIda, Tetsuji; Takasuka, Seiji; Kohno, Hitoshi; Sato, Yukiharu; Nicolaus, Beate; Boeger, Peter; Wakabayashi, Ko, 1995: Peroxidizing phytotoxic activity of 1,3,4-thiadiazolidine-2-thiones and 1,2,4-triazolidine-3,5-dithiones. Journal Of Pesticide Science. 20(1): 41-47 Using autotrophic Scenedesmus acutus cells incubated in the light and Echinochloa utilis culture, a series of isomeric compounds, namely 5-arylimino-3,4-tetramethylene-1,3,4-thiadiazolidine-2-thiones (thiadiazolidine-thiones) and 4-aryl-1,2-tetramethylene-1,2,4-triazolidine-3,5-dithiones (triazolidine-dithiones), were [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/peroxidizing-phytotoxic-activity-of-134-thiadiazolidine-2-thiones-and-124-triazolidine-35-dithiones/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Partial purification and characterization of glyoxylate oxidase from the brown-rot basidiomycete Tyromyces palustris</title><link>http://scien.net/enzyme/oxidase/partial-purification-and-characterization-of-glyoxylate-oxidase-from-the-brown-rot-basidiomycete-tyromyces-palustris</link> <comments>http://scien.net/enzyme/oxidase/partial-purification-and-characterization-of-glyoxylate-oxidase-from-the-brown-rot-basidiomycete-tyromyces-palustris#comments</comments> <pubDate>Mon, 20 May 2013 03:37:38 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[biogel]]></category> <category><![CDATA[dichloroindophenol]]></category> <category><![CDATA[glycolaldehyde]]></category> <category><![CDATA[glycollate]]></category> <category><![CDATA[glyoxal]]></category> <category><![CDATA[tyromyces]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/partial-purification-and-characterization-of-glyoxylate-oxidase-from-the-brown-rot-basidiomycete-tyromyces-palustris</guid> <description><![CDATA[Akamatsu, Y.; Shimada, M., 1994: Partial purification and characterization of glyoxylate oxidase from the brown-rot basidiomycete Tyromyces palustris. Phytochemistry (oxford). 37(3): 649-653 The glyoxylate oxidase which catalyses oxidation of glyoxylate to form oxalate and H-2o-2 was partially purified from the homogenate of a wood-destroying basidiomycete Tyromyces palustris by a combination of (Nh-4)-2so-4 precipitation, Deae-Biogel chromatography [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/partial-purification-and-characterization-of-glyoxylate-oxidase-from-the-brown-rot-basidiomycete-tyromyces-palustris/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Partial characterization of carnation petal 1-aminocyclopropane-1-carboxylate oxidase</title><link>http://scien.net/enzyme/oxidase/partial-characterization-of-carnation-petal-1-aminocyclopropane-1-carboxylate-oxidase</link> <comments>http://scien.net/enzyme/oxidase/partial-characterization-of-carnation-petal-1-aminocyclopropane-1-carboxylate-oxidase#comments</comments> <pubDate>Mon, 20 May 2013 03:37:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[aminoisobutyric]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/partial-characterization-of-carnation-petal-1-aminocyclopropane-1-carboxylate-oxidase</guid> <description><![CDATA[Nijenhus De Vries, Mariska A.; Woltering, Ernst J.; De Vrije, Truus, 1994: Partial characterization of carnation petal 1-aminocyclopropane-1-carboxylate oxidase. Journal Of Plant Physiology. 144(4-5): 549-554 The plant hormone ethylene regulates senescence in carnation flowers. The final step in the biosynthesis of ethylene i.e. the conversion of Acc to ethylene is catalysed by the enzyme Acc [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/partial-characterization-of-carnation-petal-1-aminocyclopropane-1-carboxylate-oxidase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Oxidase of the white rot fungus Panus tigrinus 8/18</title><link>http://scien.net/enzyme/oxidase/oxidase-of-the-white-rot-fungus-panus-tigrinus-818</link> <comments>http://scien.net/enzyme/oxidase/oxidase-of-the-white-rot-fungus-panus-tigrinus-818#comments</comments> <pubDate>Mon, 20 May 2013 03:31:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[abts]]></category> <category><![CDATA[coniferyl]]></category> <category><![CDATA[diaminobenzidine]]></category> <category><![CDATA[laccases]]></category> <category><![CDATA[ligninolytic]]></category> <category><![CDATA[panus]]></category> <category><![CDATA[syringaldazine]]></category> <category><![CDATA[syringic]]></category> <category><![CDATA[thioglycolate]]></category> <category><![CDATA[tigrinus]]></category> <category><![CDATA[vanillylacetone]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/oxidase-of-the-white-rot-fungus-panus-tigrinus-818</guid> <description><![CDATA[Pozdnyakova, Natalia; Leontievsky, Alexey; Golovleva, Ludmila, 1994: Oxidase of the white rot fungus Panus tigrinus 8/18. Febs Letters. 350(2-3): 194 Extracellular oxidase of the white rot fungus Panus trigrinus (earlier reported as laccase) contains copper but has no absorption spectrum typical of &#8216;blue&#8217; oxidases. Thioglycolate and sodium azide inhibit the activity of this enzyme at [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/oxidase-of-the-white-rot-fungus-panus-tigrinus-818/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Novel redox surfactants and their interactions with glucose oxidase of Aspergillus niger</title><link>http://scien.net/enzyme/oxidase/novel-redox-surfactants-and-their-interactions-with-glucose-oxidase-of-aspergillus-niger</link> <comments>http://scien.net/enzyme/oxidase/novel-redox-surfactants-and-their-interactions-with-glucose-oxidase-of-aspergillus-niger#comments</comments> <pubDate>Mon, 20 May 2013 03:10:38 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[cmcs]]></category> <category><![CDATA[dipyridylamine]]></category> <category><![CDATA[nonsurfactant]]></category> <category><![CDATA[physisorption]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/novel-redox-surfactants-and-their-interactions-with-glucose-oxidase-of-aspergillus-niger</guid> <description><![CDATA[Saudan, Pascale; Zakeeruddin, Shaik Mohammed; Malavallon, Muriell Anne; Gratzel, Michael; Fraser, David Michael, 1994: Novel redox surfactants and their interactions with glucose oxidase of Aspergillus niger. Biotechnology &#038; Bioengineering. 44(4): 407-418 A number of novel redox surfactants (based on mixed bipyridine/dipyridylamine complexes of osmium where the dipyridylamine ligand bears a saturated C-8, C-10, C-12, C-14, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/novel-redox-surfactants-and-their-interactions-with-glucose-oxidase-of-aspergillus-niger/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Novel approaches for the use of mediators in enzyme electrodes</title><link>http://scien.net/enzyme/oxidase/novel-approaches-for-the-use-of-mediators-in-enzyme-electrodes</link> <comments>http://scien.net/enzyme/oxidase/novel-approaches-for-the-use-of-mediators-in-enzyme-electrodes#comments</comments> <pubDate>Mon, 20 May 2013 03:10:16 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[evaporates]]></category> <category><![CDATA[ferricinium]]></category> <category><![CDATA[ferrocene]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/novel-approaches-for-the-use-of-mediators-in-enzyme-electrodes</guid> <description><![CDATA[Rosen Margalit, Ilana; Rishpon, Judith, 1993: Novel approaches for the use of mediators in enzyme electrodes. Biosensors &#038; Bioelectronics. 8(6): 315-323 This work describes the preparation of glucose electrodes consisting of an enzyme (glucose oxidase) and a mediator embedded in a colloidal graphite emulsion matrix. These components are homogeneously mixed in an organic medium that [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/novel-approaches-for-the-use-of-mediators-in-enzyme-electrodes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Nature and regulation of pistil-expressed genes in tomato</title><link>http://scien.net/enzyme/oxidase/nature-and-regulation-of-pistil-expressed-genes-in-tomato</link> <comments>http://scien.net/enzyme/oxidase/nature-and-regulation-of-pistil-expressed-genes-in-tomato#comments</comments> <pubDate>Mon, 20 May 2013 02:57:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[aminopeptidases]]></category> <category><![CDATA[endomembrane]]></category> <category><![CDATA[hyoscyamine]]></category> <category><![CDATA[miraculin]]></category> <category><![CDATA[thionin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/nature-and-regulation-of-pistil-expressed-genes-in-tomato</guid> <description><![CDATA[Milligan, Sb; Gasser, Cs, 1995: Nature and regulation of pistil-expressed genes in tomato. Plant molecular biology 28(4): 691-711 The specialized reproductive functions of angiosperm pistils are dependent in part upon the regulated activation of numerous genes expressed predominantly in this organ system. To better understand the nature of these pistil-predominant gene products we have analyzed [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/nature-and-regulation-of-pistil-expressed-genes-in-tomato/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Molecular properties and myocardial salvage effects of morin hydrate</title><link>http://scien.net/enzyme/oxidase/molecular-properties-and-myocardial-salvage-effects-of-morin-hydrate</link> <comments>http://scien.net/enzyme/oxidase/molecular-properties-and-myocardial-salvage-effects-of-morin-hydrate#comments</comments> <pubDate>Mon, 20 May 2013 02:43:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[coplanarity]]></category> <category><![CDATA[delocalization]]></category> <category><![CDATA[morin]]></category> <category><![CDATA[oxyradical]]></category> <category><![CDATA[oxyradicals]]></category> <category><![CDATA[scavenges]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/molecular-properties-and-myocardial-salvage-effects-of-morin-hydrate</guid> <description><![CDATA[Wu, Tai Wing; Fung, Kwok Pui; Zeng, Ling Hua; Wu, Jun; HempelAndrew; Grey, Arthru A.; Camerman, Norman, 1995: Molecular properties and myocardial salvage effects of morin hydrate. Biochemical Pharmacology. 49(4): 537-543 Morin hydrate is a bioactive pigment found in yellow Brazil wood. Recently, we reported that morin hydrate prolongs the survival of three types of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/molecular-properties-and-myocardial-salvage-effects-of-morin-hydrate/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Mixed function oxidase system in hepatic and extrahepatic tissues of developing chickens following various treatments</title><link>http://scien.net/enzyme/oxidase/mixed-function-oxidase-system-in-hepatic-and-extrahepatic-tissues-of-developing-chickens-following-various-treatments</link> <comments>http://scien.net/enzyme/oxidase/mixed-function-oxidase-system-in-hepatic-and-extrahepatic-tissues-of-developing-chickens-following-various-treatments#comments</comments> <pubDate>Mon, 20 May 2013 02:33:22 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/mixed-function-oxidase-system-in-hepatic-and-extrahepatic-tissues-of-developing-chickens-following-various-treatments</guid> <description><![CDATA[Hatolkar, V. S.; Pawer, S. S., 1995: Mixed function oxidase system in hepatic and extrahepatic tissues of developing chickens following various treatments. Indian Journal Of Experimental Biology. 33(1): 48-50 Alterations in hepatic and extrahepatic protein content, activities of drug enzymes, lipid peroxidation and hydrogen peroxide formation and levels of microsomal electron transport components were examined [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/mixed-function-oxidase-system-in-hepatic-and-extrahepatic-tissues-of-developing-chickens-following-various-treatments/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Metabolic alterations in cotyledons of Cucurbita pepo infected by cucumber mosaic virus</title><link>http://scien.net/enzyme/oxidase/metabolic-alterations-in-cotyledons-of-cucurbita-pepo-infected-by-cucumber-mosaic-virus</link> <comments>http://scien.net/enzyme/oxidase/metabolic-alterations-in-cotyledons-of-cucurbita-pepo-infected-by-cucumber-mosaic-virus#comments</comments> <pubDate>Mon, 20 May 2013 02:23:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[anaplerotic]]></category> <category><![CDATA[glycerate]]></category> <category><![CDATA[hydratase]]></category> <category><![CDATA[hydroxypyruvate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/metabolic-alterations-in-cotyledons-of-cucurbita-pepo-infected-by-cucumber-mosaic-virus</guid> <description><![CDATA[Tecsi, Laszlo I.; Maule, Andy J.; Smith, Alison M.; Leegood, Richard C., 1994: Metabolic alterations in cotyledons of Cucurbita pepo infected by cucumber mosaic virus. Journal Of Experimental Botany. 45(280): 1541-1551 Changes in the capacities of enzymes in various metabolic pathways have been measured during infection of cotyledons of Cucurbita pepo L. with cucumber mosaic [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/metabolic-alterations-in-cotyledons-of-cucurbita-pepo-infected-by-cucumber-mosaic-virus/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Localization of phenol oxidase in female Trichuris suis</title><link>http://scien.net/enzyme/oxidase/localization-of-phenol-oxidase-in-female-trichuris-suis</link> <comments>http://scien.net/enzyme/oxidase/localization-of-phenol-oxidase-in-female-trichuris-suis#comments</comments> <pubDate>Mon, 20 May 2013 02:03:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[diphenols]]></category> <category><![CDATA[methylcatechol]]></category> <category><![CDATA[stichosome]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/localization-of-phenol-oxidase-in-female-trichuris-suis</guid> <description><![CDATA[Fetterer, Raymond H.; Hill, Dolores E., 1994: Localization of phenol oxidase in female Trichuris suis. Journal Of Parasitology. 80(6): 952-959 A phenol oxidase (E.C. 1.10.3.1) preparation from adult female Trichuris suis was assayed by both polarographic and spectrophotometric techniques. The T. suis enzyme oxidized most diphenols including 4-methylcatechol (4mc) and dihydroxyphenylalanine but did not oxidize [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/localization-of-phenol-oxidase-in-female-trichuris-suis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Isolation of a lignolytic bacterium for the degradation and possible utilization of coir waste</title><link>http://scien.net/enzyme/oxidase/isolation-of-a-lignolytic-bacterium-for-the-degradation-and-possible-utilization-of-coir-waste</link> <comments>http://scien.net/enzyme/oxidase/isolation-of-a-lignolytic-bacterium-for-the-degradation-and-possible-utilization-of-coir-waste#comments</comments> <pubDate>Sun, 19 May 2013 05:52:39 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[coir]]></category> <category><![CDATA[ligninase]]></category> <category><![CDATA[lignolytic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/isolation-of-a-lignolytic-bacterium-for-the-degradation-and-possible-utilization-of-coir-waste</guid> <description><![CDATA[Uma, L; Kalaiselvi, R; Subramanian, G., 1994: Isolation of a lignolytic bacterium for the degradation and possible utilization of coir waste. Biotechnology letters 16(3): 303-308 Coir, fibre of coconut used for making ropes results in the accumulation of huge quantities of lignin waste. Enrichment technique yielded a lignin a degrading bacterium characterized as Pseudomonas sp. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/isolation-of-a-lignolytic-bacterium-for-the-degradation-and-possible-utilization-of-coir-waste/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants</title><link>http://scien.net/enzyme/oxidase/investigation-of-the-subcellular-location-of-the-tetrapyrrole-biosynthesis-enzyme-coproporphyrinogen-oxidase-in-higher-plants</link> <comments>http://scien.net/enzyme/oxidase/investigation-of-the-subcellular-location-of-the-tetrapyrrole-biosynthesis-enzyme-coproporphyrinogen-oxidase-in-higher-plants#comments</comments> <pubDate>Sun, 19 May 2013 05:42:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[arum]]></category> <category><![CDATA[coprogen]]></category> <category><![CDATA[coproporphyrinogen]]></category> <category><![CDATA[etioplasts]]></category> <category><![CDATA[fluorimetrically]]></category> <category><![CDATA[protogen]]></category> <category><![CDATA[protoporphyrinogen]]></category> <category><![CDATA[spadices]]></category> <category><![CDATA[tetrapyrrole]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/investigation-of-the-subcellular-location-of-the-tetrapyrrole-biosynthesis-enzyme-coproporphyrinogen-oxidase-in-higher-plants</guid> <description><![CDATA[Smith, Ag; Marsh, O; Elder, Gh, 1993: Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochemical journal, 292(2): 503-508 The subcellular location of two enzymes in the biosynthetic pathway for protoporphyrin Ix, coproporphyrinogen (coprogen) oxidase (Ec 1.3.3.3) and protoporphyrinogen (protogen) oxidase (Ec 1.3.3.4) has been investigated in etiolated pea [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/investigation-of-the-subcellular-location-of-the-tetrapyrrole-biosynthesis-enzyme-coproporphyrinogen-oxidase-in-higher-plants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Interactive potential of omega-3 fatty acids with clofibrate or DEHP on hepatic peroxisome proliferation in male Wistar rats</title><link>http://scien.net/enzyme/oxidase/interactive-potential-of-omega-3-fatty-acids-with-clofibrate-or-dehp-on-hepatic-peroxisome-proliferation-in-male-wistar-rats</link> <comments>http://scien.net/enzyme/oxidase/interactive-potential-of-omega-3-fatty-acids-with-clofibrate-or-dehp-on-hepatic-peroxisome-proliferation-in-male-wistar-rats#comments</comments> <pubDate>Sun, 19 May 2013 05:36:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[dehp]]></category> <category><![CDATA[ethylhexylphthalate]]></category> <category><![CDATA[menhaden]]></category> <category><![CDATA[proliferators]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/interactive-potential-of-omega-3-fatty-acids-with-clofibrate-or-dehp-on-hepatic-peroxisome-proliferation-in-male-wistar-rats</guid> <description><![CDATA[Wysynski, Anna Marie; Baldwin, Linda A.; Leonard, Denise A.; Calabrese, Edward J., 1993: Interactive potential of omega-3 fatty acids with clofibrate or DEHP on hepatic peroxisome proliferation in male Wistar rats. Human &#038; Experimental Toxicology. 12(4): 337-340 The interactive potential of three known peroxisome proliferators, omega-3 fatty acids, clofibrate and di(2-ethylhexylphthalate (Dehp), was evaluated in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/interactive-potential-of-omega-3-fatty-acids-with-clofibrate-or-dehp-on-hepatic-peroxisome-proliferation-in-male-wistar-rats/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of exogenous hormones on the growth and secondary metabolite formation in transformed root cultures</title><link>http://scien.net/enzyme/oxidase/influence-of-exogenous-hormones-on-the-growth-and-secondary-metabolite-formation-in-transformed-root-cultures</link> <comments>http://scien.net/enzyme/oxidase/influence-of-exogenous-hormones-on-the-growth-and-secondary-metabolite-formation-in-transformed-root-cultures#comments</comments> <pubDate>Sun, 19 May 2013 05:10:12 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[brugmansia]]></category> <category><![CDATA[disorganisation]]></category> <category><![CDATA[tropane]]></category> <category><![CDATA[tropine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/influence-of-exogenous-hormones-on-the-growth-and-secondary-metabolite-formation-in-transformed-root-cultures</guid> <description><![CDATA[&#8220;Rhodes, M. J. C.; Parr, A. J.; Giulietti, A.; Aird, E. L. H., 1994: Influence of exogenous hormones on the growth and secondary metabolite formation in transformed root cultures. Plant Cell Tissue &#038; Organ Culture. 38(2-3): 143-151 Transformed organ cultures formed following transformation of plant tissues with Agrobacterium species owe their phenotypes to alterations in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/influence-of-exogenous-hormones-on-the-growth-and-secondary-metabolite-formation-in-transformed-root-cultures/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of CO2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seedlings</title><link>http://scien.net/enzyme/oxidase/influence-of-co2-on-acc-oxidase-activity-from-roots-of-sunflower-helianthus-annuus-seedlings</link> <comments>http://scien.net/enzyme/oxidase/influence-of-co2-on-acc-oxidase-activity-from-roots-of-sunflower-helianthus-annuus-seedlings#comments</comments> <pubDate>Sun, 19 May 2013 05:06:34 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/influence-of-co2-on-acc-oxidase-activity-from-roots-of-sunflower-helianthus-annuus-seedlings</guid> <description><![CDATA[Finlayson, S. A.; Reid, D. M., 1994: Influence of CO2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seedlings. Phytochemistry 35(4): 847-851 The activity of the ethylene forming enzyme Acc oxidase was assayed in vitro under aerobic conditions with and without high levels of exogenous Co2, varying the parameters of ascorbate, pH, temperature, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/influence-of-co2-on-acc-oxidase-activity-from-roots-of-sunflower-helianthus-annuus-seedlings/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Induction of hepatic drug metabolizing enzymes and interaction with carbon tetrachloride in rats after a single oral exposure to atrazine</title><link>http://scien.net/enzyme/oxidase/induction-of-hepatic-drug-metabolizing-enzymes-and-interaction-with-carbon-tetrachloride-in-rats-after-a-single-oral-exposure-to-atrazine</link> <comments>http://scien.net/enzyme/oxidase/induction-of-hepatic-drug-metabolizing-enzymes-and-interaction-with-carbon-tetrachloride-in-rats-after-a-single-oral-exposure-to-atrazine#comments</comments> <pubDate>Sun, 19 May 2013 05:03:10 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[dealkylase]]></category> <category><![CDATA[hexobarbital]]></category> <category><![CDATA[pentoxyresorufin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/induction-of-hepatic-drug-metabolizing-enzymes-and-interaction-with-carbon-tetrachloride-in-rats-after-a-single-oral-exposure-to-atrazine</guid> <description><![CDATA[Ugazio, Giancarlo; Burdino, Elisa; Dacasto, Mauro; Bosio, Anita; Van T.Klooster, Gerben; Nebbia, Carlo, 1993: Induction of hepatic drug metabolizing enzymes and interaction with carbon tetrachloride in rats after a single oral exposure to atrazine. Toxicology Letters (amsterdam). 69(3): 279-288 A single oral dose (430 mg/kg) of atrazine, a widely employed s-triazine herbicide, was administered to [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/induction-of-hepatic-drug-metabolizing-enzymes-and-interaction-with-carbon-tetrachloride-in-rats-after-a-single-oral-exposure-to-atrazine/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>In vitro activation of grape polyphenol oxidase by polyglucan type elicitors</title><link>http://scien.net/enzyme/oxidase/in-vitro-activation-of-grape-polyphenol-oxidase-by-polyglucan-type-elicitors</link> <comments>http://scien.net/enzyme/oxidase/in-vitro-activation-of-grape-polyphenol-oxidase-by-polyglucan-type-elicitors#comments</comments> <pubDate>Sun, 19 May 2013 04:28:54 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[gamay]]></category> <category><![CDATA[polycationic]]></category> <category><![CDATA[polyglucan]]></category> <category><![CDATA[polyglucans]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/in-vitro-activation-of-grape-polyphenol-oxidase-by-polyglucan-type-elicitors</guid> <description><![CDATA[Jimenez, Mercedes; Garcia Carmona, Francisco, 1993: In vitro activation of grape polyphenol oxidase by polyglucan type elicitors. Plant Physiology &#038; Biochemistry (montrouge). 31(4): 541-546 Latent polyphenol oxidase, extracted and partially purified from grapevine (Vitis vinifera L. cv. Gamay) cell suspension cultures, was shown to be activated by the polyglucans zymosan and chitosan. Activation increased with [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/in-vitro-activation-of-grape-polyphenol-oxidase-by-polyglucan-type-elicitors/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Immunochemical and immunohistochemical study of apple chlorogenic acid oxidase</title><link>http://scien.net/enzyme/oxidase/immunochemical-and-immunohistochemical-study-of-apple-chlorogenic-acid-oxidase</link> <comments>http://scien.net/enzyme/oxidase/immunochemical-and-immunohistochemical-study-of-apple-chlorogenic-acid-oxidase#comments</comments> <pubDate>Sun, 19 May 2013 04:20:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[immunocytolocalization]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/immunochemical-and-immunohistochemical-study-of-apple-chlorogenic-acid-oxidase</guid> <description><![CDATA[Murata, Masatsune; Kurokami, Chiyo; Homma, Seiichi; Matsuhashi, Choku, 1993: Immunochemical and immunohistochemical study of apple chlorogenic acid oxidase. Journal Of Agricultural &#038; Food Chemistry. 41(9): 1385-1390 Mouse antibody was raised against chlorogenic acid oxidase from apple (Malus pumila cv. Fuji). This antiserum was used for immunochemical characterization of the enzyme of apple and other plants [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/immunochemical-and-immunohistochemical-study-of-apple-chlorogenic-acid-oxidase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Identification and characterization of an auxin-degrading enzyme in downy mildew infected sunflower</title><link>http://scien.net/enzyme/oxidase/identification-and-characterization-of-an-auxin-degrading-enzyme-in-downy-mildew-infected-sunflower</link> <comments>http://scien.net/enzyme/oxidase/identification-and-characterization-of-an-auxin-degrading-enzyme-in-downy-mildew-infected-sunflower#comments</comments> <pubDate>Sun, 19 May 2013 04:12:01 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[berl]]></category> <category><![CDATA[halstedii]]></category> <category><![CDATA[monophenols]]></category> <category><![CDATA[scopoletin]]></category> <category><![CDATA[toni]]></category> <category><![CDATA[triiodobenzoic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/identification-and-characterization-of-an-auxin-degrading-enzyme-in-downy-mildew-infected-sunflower</guid> <description><![CDATA[Benz, A.; Spring, O., 1995: Identification and characterization of an auxin-degrading enzyme in downy mildew infected sunflower. Physiological &#038; Molecular Plant Pathology. 46(3): 163-175 An auxin-metabolizing enzyme was purified from growth-retarded sunflower plants (Helianthus annuus L.) infected with downy mildew (Plasmopara halstedii (Far).) Berl. et de Toni) by means of differential centrifugation, salt precipitation and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/identification-and-characterization-of-an-auxin-degrading-enzyme-in-downy-mildew-infected-sunflower/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Hydrogen-peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase</title><link>http://scien.net/enzyme/oxidase/hydrogen-peroxide-producing-system-of-pleurotus-eryngii-involving-the-extracellular-enzyme-aryl-alcohol-oxidase</link> <comments>http://scien.net/enzyme/oxidase/hydrogen-peroxide-producing-system-of-pleurotus-eryngii-involving-the-extracellular-enzyme-aryl-alcohol-oxidase#comments</comments> <pubDate>Sun, 19 May 2013 04:08:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category> <category><![CDATA[eryngii]]></category> <category><![CDATA[ligninolytic]]></category> <category><![CDATA[multienzymatic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/hydrogen-peroxide-producing-system-of-pleurotus-eryngii-involving-the-extracellular-enzyme-aryl-alcohol-oxidase</guid> <description><![CDATA[Guillen, F; Martinez, At; Martinez, Mj; Evans, Cs, 1994: Hydrogen-peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase. Applied microbiology and biotechnology 41(4): 465-470 The effect of benzyl alcohol, benzaldehyde and benzoic acid on the production of extracellular hydrogen peroxide (H2o2) by the ligninolytic fungus Pleurotus eryngii was investigated. It was found that [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/hydrogen-peroxide-producing-system-of-pleurotus-eryngii-involving-the-extracellular-enzyme-aryl-alcohol-oxidase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>High level production of recombinant invertase in Hansenula polymorpha</title><link>http://scien.net/enzyme/oxidase/high-level-production-of-recombinant-invertase-in-hansenula-polymorpha</link> <comments>http://scien.net/enzyme/oxidase/high-level-production-of-recombinant-invertase-in-hansenula-polymorpha#comments</comments> <pubDate>Sun, 19 May 2013 03:59:07 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Oxidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/oxidase/high-level-production-of-recombinant-invertase-in-hansenula-polymorpha</guid> <description><![CDATA[Narciandi, Re; Rodriguez, L; Rodriguez, E; Diaz, R; Delgado, J; Herrera, L., 1995: High level production of recombinant invertase in Hansenula polymorpha. Biotechnology letters 17(9): 949-952 The Suc 2 gene from Saccharomyces cerevisiae coding for the enzyme Invertase was cloned in Hansenula polymorpha under the control of the alcohol-oxidase (Aox) promoter of Pichia pastoris. The [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/oxidase/high-level-production-of-recombinant-invertase-in-hansenula-polymorpha/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>