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><channel><title>Natural Sciences Bibliography &#187; Dehydrogenase</title> <atom:link href="http://scien.net/category/enzyme/dehydrogenase/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>195,000 References and 135,000 Tags</description> <lastBuildDate>Sun, 19 May 2013 06:07:22 +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>Isozyme diversity in sour, sweet, and ground cherry</title><link>http://scien.net/enzyme/dehydrogenase/isozyme-diversity-in-sour-sweet-and-ground-cherry</link> <comments>http://scien.net/enzyme/dehydrogenase/isozyme-diversity-in-sour-sweet-and-ground-cherry#comments</comments> <pubDate>Sun, 19 May 2013 05:56:11 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[cerasus]]></category> <category><![CDATA[phosphoglucose]]></category> <category><![CDATA[shikimate]]></category> <category><![CDATA[skdh]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/isozyme-diversity-in-sour-sweet-and-ground-cherry</guid> <description><![CDATA[Beaver, Ja; Iezzoni, Af; Ramm, Cw, 1995: Isozyme diversity in sour, sweet, and ground cherry. Theoretical and applied genetics 90(6): 847-852 Thirty-six sour (Prunus cerasus L.), sweet (P. avium L.), and ground cherry (P. fruticosa Pall.) selections were evaluated for seven enzyme systems and principal coordinate analysis was used to examine isozyme divergence among these [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/isozyme-diversity-in-sour-sweet-and-ground-cherry/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Isolation of apoplasmic fluid from sunflower leaves and its use for studies on influence of nitrogen supply on apoplasmic pH</title><link>http://scien.net/enzyme/dehydrogenase/isolation-of-apoplasmic-fluid-from-sunflower-leaves-and-its-use-for-studies-on-influence-of-nitrogen-supply-on-apoplasmic-ph</link> <comments>http://scien.net/enzyme/dehydrogenase/isolation-of-apoplasmic-fluid-from-sunflower-leaves-and-its-use-for-studies-on-influence-of-nitrogen-supply-on-apoplasmic-ph#comments</comments> <pubDate>Sun, 19 May 2013 05:53:14 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[apoplasmic]]></category> <category><![CDATA[sulphorhodamine]]></category> <category><![CDATA[symplasmic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/isolation-of-apoplasmic-fluid-from-sunflower-leaves-and-its-use-for-studies-on-influence-of-nitrogen-supply-on-apoplasmic-ph</guid> <description><![CDATA[Dannel, Frank; Pfeffer, Heidrun; Marschner, Horst, 1995: Isolation of apoplasmic fluid from sunflower leaves and its use for studies on influence of nitrogen supply on apoplasmic pH. Journal Of Plant Physiology. 146(3): 273-273 A centrifugation method for collection of apoplasmic fluid from isolated sunflower leaves has been developed. As indicated by the marker enzymes hexose [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/isolation-of-apoplasmic-fluid-from-sunflower-leaves-and-its-use-for-studies-on-influence-of-nitrogen-supply-on-apoplasmic-ph/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Isoelectric focusing isozyme profiles and taxonomic distances among Fusarium species of the sections Arthrosporiella and Sporotrichiella</title><link>http://scien.net/enzyme/dehydrogenase/isoelectric-focusing-isozyme-profiles-and-taxonomic-distances-among-fusarium-species-of-the-sections-arthrosporiella-and-sporotrichiella</link> <comments>http://scien.net/enzyme/dehydrogenase/isoelectric-focusing-isozyme-profiles-and-taxonomic-distances-among-fusarium-species-of-the-sections-arthrosporiella-and-sporotrichiella#comments</comments> <pubDate>Sun, 19 May 2013 05:47:30 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[arthrosporiella]]></category> <category><![CDATA[avenaceum]]></category> <category><![CDATA[camptoceras]]></category> <category><![CDATA[chlamydosporum]]></category> <category><![CDATA[citriform]]></category> <category><![CDATA[microconidia]]></category> <category><![CDATA[pallidoroseum]]></category> <category><![CDATA[phosphoglucose]]></category> <category><![CDATA[poae]]></category> <category><![CDATA[sporotrichiella]]></category> <category><![CDATA[tricinctum]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/isoelectric-focusing-isozyme-profiles-and-taxonomic-distances-among-fusarium-species-of-the-sections-arthrosporiella-and-sporotrichiella</guid> <description><![CDATA[Pomazi, Andrea; Hornok, L.; Szecsi, A., 1993: Isoelectric focusing isozyme profiles and taxonomic distances among Fusarium species of the sections Arthrosporiella and Sporotrichiella. Acta Microbiologica Hungarica. 40(1): 71-79 Isozymes from 18 isolates representing seven species of the Fusarium sections Arthrosporiella and Sporotrichiella were compared by isoelectric focusing in polyacrylamide gels. Of the six enzyme systems [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/isoelectric-focusing-isozyme-profiles-and-taxonomic-distances-among-fusarium-species-of-the-sections-arthrosporiella-and-sporotrichiella/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Introgression of the Florida largemouth bass genome into stream populations of northern largemouth bass in Oklahoma</title><link>http://scien.net/enzyme/dehydrogenase/introgression-of-the-florida-largemouth-bass-genome-into-stream-populations-of-northern-largemouth-bass-in-oklahoma</link> <comments>http://scien.net/enzyme/dehydrogenase/introgression-of-the-florida-largemouth-bass-genome-into-stream-populations-of-northern-largemouth-bass-in-oklahoma#comments</comments> <pubDate>Sun, 19 May 2013 05:41:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[floridanus]]></category> <category><![CDATA[interbreeding]]></category> <category><![CDATA[intergrades]]></category> <category><![CDATA[introgressed]]></category> <category><![CDATA[saat]]></category> <category><![CDATA[salmoides]]></category> <category><![CDATA[seining]]></category> <category><![CDATA[sidhp]]></category> <category><![CDATA[smdh]]></category> <category><![CDATA[ssod]]></category> <category><![CDATA[supplementally]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/introgression-of-the-florida-largemouth-bass-genome-into-stream-populations-of-northern-largemouth-bass-in-oklahoma</guid> <description><![CDATA[Gelwick, Frances P.; Gilliland, Eugene R.; Matthews, William J., 1995: Introgression of the Florida largemouth bass genome into stream populations of northern largemouth bass in Oklahoma. Transactions Of The American Fisheries Society. 124(4): 550-562 Oklahoma streams and reservoirs historically contained only the northern subspecies of largemouth bass Micropterus salmoides salmoides. From 1970 to 1991 Oklahoma [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/introgression-of-the-florida-largemouth-bass-genome-into-stream-populations-of-northern-largemouth-bass-in-oklahoma/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Intracellular binding of glucokinase in hepatocytes and translocation by glucose, fructose and insulin</title><link>http://scien.net/enzyme/dehydrogenase/intracellular-binding-of-glucokinase-in-hepatocytes-and-translocation-by-glucose-fructose-and-insulin</link> <comments>http://scien.net/enzyme/dehydrogenase/intracellular-binding-of-glucokinase-in-hepatocytes-and-translocation-by-glucose-fructose-and-insulin#comments</comments> <pubDate>Sun, 19 May 2013 05:39:34 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[phosphoglucoisomerase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/intracellular-binding-of-glucokinase-in-hepatocytes-and-translocation-by-glucose-fructose-and-insulin</guid> <description><![CDATA[Agius, Loranne; Peak, Matthew, 1993: Intracellular binding of glucokinase in hepatocytes and translocation by glucose, fructose and insulin. Biochemical Journal. 296(3): 785-796 The release of glucokinase from digitonin-permeabilized hepatocytes shows different characteristics with respect to ionic strength and (MgCl-2) from the release of other cytoplasmic enzymes. Release of glucokinase is most rapid at low ionic [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/intracellular-binding-of-glucokinase-in-hepatocytes-and-translocation-by-glucose-fructose-and-insulin/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Inhibitors of de novo fatty acid biosynthesis in higher plants</title><link>http://scien.net/enzyme/dehydrogenase/inhibitors-of-de-novo-fatty-acid-biosynthesis-in-higher-plants</link> <comments>http://scien.net/enzyme/dehydrogenase/inhibitors-of-de-novo-fatty-acid-biosynthesis-in-higher-plants#comments</comments> <pubDate>Sun, 19 May 2013 05:27:09 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[acetylmethyl]]></category> <category><![CDATA[adenylates]]></category> <category><![CDATA[cerulenin]]></category> <category><![CDATA[ketoacyl]]></category> <category><![CDATA[phosphinate]]></category> <category><![CDATA[plastidic]]></category> <category><![CDATA[thiolactomycin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/inhibitors-of-de-novo-fatty-acid-biosynthesis-in-higher-plants</guid> <description><![CDATA[Golz, Andrea; Focke, Manfred; Lichtenthaler, Hartmut K., 1994: Inhibitors of de novo fatty acid biosynthesis in higher plants. Journal Of Plant Physiology. 143(4-5): 426-433 The present knowledge of de novo fatty acid biosynthesis in plastids of higher plants is reviewed with respect to its inhibition by various synthetic and natural xenobiotics. Certain enzymatic steps In [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/inhibitors-of-de-novo-fatty-acid-biosynthesis-in-higher-plants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Inhibition of the plastidic pyruvate dehydrogenase complex in isolated plastids of oat</title><link>http://scien.net/enzyme/dehydrogenase/inhibition-of-the-plastidic-pyruvate-dehydrogenase-complex-in-isolated-plastids-of-oat</link> <comments>http://scien.net/enzyme/dehydrogenase/inhibition-of-the-plastidic-pyruvate-dehydrogenase-complex-in-isolated-plastids-of-oat#comments</comments> <pubDate>Sun, 19 May 2013 05:26:48 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[ampi]]></category> <category><![CDATA[etioplasts]]></category> <category><![CDATA[plastidic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/inhibition-of-the-plastidic-pyruvate-dehydrogenase-complex-in-isolated-plastids-of-oat</guid> <description><![CDATA[Golz, Andrea; Lichtenthaler, Hartmut K., 1994: Inhibition of the plastidic pyruvate dehydrogenase complex in isolated plastids of oat. Zeitschrift Fuer Naturforschung Section C Biosciences. 49(7-8): 421-426 The activity of the plastidic pyruvate dehydrogenase complex (pPDHC) is one source of acetyl-CoA in plastids of higher plants needed for de novo fatty acid biosynthesis. This plastidic enzyme [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/inhibition-of-the-plastidic-pyruvate-dehydrogenase-complex-in-isolated-plastids-of-oat/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of the form of nitrogen on ammonium, amino acids and N-assimilating enzyme activity in maize genotypes</title><link>http://scien.net/enzyme/dehydrogenase/influence-of-the-form-of-nitrogen-on-ammonium-amino-acids-and-n-assimilating-enzyme-activity-in-maize-genotypes</link> <comments>http://scien.net/enzyme/dehydrogenase/influence-of-the-form-of-nitrogen-on-ammonium-amino-acids-and-n-assimilating-enzyme-activity-in-maize-genotypes#comments</comments> <pubDate>Sun, 19 May 2013 05:18:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[unbuffered]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/influence-of-the-form-of-nitrogen-on-ammonium-amino-acids-and-n-assimilating-enzyme-activity-in-maize-genotypes</guid> <description><![CDATA[Magalhaes, J. R.; Huber, D. M.; Tsai, C. Y., 1995: Influence of the form of nitrogen on ammonium, amino acids and N-assimilating enzyme activity in maize genotypes. Journal Of Plant Nutrition. 18(4): 747-763 An understanding of nitrogen (N) interactions with plant growth and metabolism is important in order to increase the efficiency of fertilizer amendments [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/influence-of-the-form-of-nitrogen-on-ammonium-amino-acids-and-n-assimilating-enzyme-activity-in-maize-genotypes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of phosphate fertilization on fungal alkaline phosphatase and succinate dehydrogenase activities in arbuscular mycorrhiza of soybean and pineapple</title><link>http://scien.net/enzyme/dehydrogenase/influence-of-phosphate-fertilization-on-fungal-alkaline-phosphatase-and-succinate-dehydrogenase-activities-in-arbuscular-mycorrhiza-of-soybean-and-pineapple</link> <comments>http://scien.net/enzyme/dehydrogenase/influence-of-phosphate-fertilization-on-fungal-alkaline-phosphatase-and-succinate-dehydrogenase-activities-in-arbuscular-mycorrhiza-of-soybean-and-pineapple#comments</comments> <pubDate>Sun, 19 May 2013 05:14:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[endomycorrhizal]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/influence-of-phosphate-fertilization-on-fungal-alkaline-phosphatase-and-succinate-dehydrogenase-activities-in-arbuscular-mycorrhiza-of-soybean-and-pineapple</guid> <description><![CDATA[Guillemin, J. P.; Orozco, M. O.; Gianinazzi Pearson, V.; Gianinazzi, S., 1995: Influence of phosphate fertilization on fungal alkaline phosphatase and succinate dehydrogenase activities in arbuscular mycorrhiza of soybean and pineapple. Agriculture Ecosystems &#038; Environment. 53(1): 63-69 Effects of phosphate fertilization on the physiological activity of arbuscular mycorrhizal infection were studied using fungal succinate dehydrogenase [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/influence-of-phosphate-fertilization-on-fungal-alkaline-phosphatase-and-succinate-dehydrogenase-activities-in-arbuscular-mycorrhiza-of-soybean-and-pineapple/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of dietary medium- and long-chain triglycerides on fat deposition and lipogenic enzyme activities in rats</title><link>http://scien.net/enzyme/dehydrogenase/influence-of-dietary-medium-and-long-chain-triglycerides-on-fat-deposition-and-lipogenic-enzyme-activities-in-rats</link> <comments>http://scien.net/enzyme/dehydrogenase/influence-of-dietary-medium-and-long-chain-triglycerides-on-fat-deposition-and-lipogenic-enzyme-activities-in-rats#comments</comments> <pubDate>Sun, 19 May 2013 05:09:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[isocalorically]]></category> <category><![CDATA[mcfa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/influence-of-dietary-medium-and-long-chain-triglycerides-on-fat-deposition-and-lipogenic-enzyme-activities-in-rats</guid> <description><![CDATA[Hwang, S. G.; Yano, H.; Kawashima, R., 1993: Influence of dietary medium- and long-chain triglycerides on fat deposition and lipogenic enzyme activities in rats. Journal Of The American College Of Nutrition. 12(6): 643-650 The present study investigates fat deposition, variances of fatty acid (Fa) composition, and lipogenic enzyme activities through dietary medium- and long-chain triglyceride [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/influence-of-dietary-medium-and-long-chain-triglycerides-on-fat-deposition-and-lipogenic-enzyme-activities-in-rats/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of cropping systems on soil biochemical properties in an arid rain-fed environment</title><link>http://scien.net/enzyme/dehydrogenase/influence-of-cropping-systems-on-soil-biochemical-properties-in-an-arid-rain-fed-environment</link> <comments>http://scien.net/enzyme/dehydrogenase/influence-of-cropping-systems-on-soil-biochemical-properties-in-an-arid-rain-fed-environment#comments</comments> <pubDate>Sun, 19 May 2013 05:08:29 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[clusterbean]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/influence-of-cropping-systems-on-soil-biochemical-properties-in-an-arid-rain-fed-environment</guid> <description><![CDATA[Rao, A. V.; Tarafdar, J. C.; Sharma, S. K.; Praveen Kumar; Aggarwal, R. K., 1995: Influence of cropping systems on soil biochemical properties in an arid rain-fed environment. Journal Of Arid Environments. 31(2): 237-244 The effect of eight crop rotations was studied for 3 years (1990-92) on enzyme activities, nitrifying bacteria, Vam spores, organic matter, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/influence-of-cropping-systems-on-soil-biochemical-properties-in-an-arid-rain-fed-environment/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Influence of chloride and sulphate ions on soil enzymes</title><link>http://scien.net/enzyme/dehydrogenase/influence-of-chloride-and-sulphate-ions-on-soil-enzymes</link> <comments>http://scien.net/enzyme/dehydrogenase/influence-of-chloride-and-sulphate-ions-on-soil-enzymes#comments</comments> <pubDate>Sun, 19 May 2013 05:08:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/influence-of-chloride-and-sulphate-ions-on-soil-enzymes</guid> <description><![CDATA[Dinesh, R.; Ramanathan, G.; Singh, Harjit, 1995: Influence of chloride and sulphate ions on soil enzymes. Journal Of Agronomy &#038; Crop Science. 175(2): 129-133 Ammonium chloride (Ac) and ammonium sulphate (As) are commonly used nitrogen fertilizers. But the effect of chloride and sulphate ions from these fertilizers on soil enzyme activity has received scant attention. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/influence-of-chloride-and-sulphate-ions-on-soil-enzymes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>In vivo mitochondrial pyruvate dehydrogenase activity, studied by rapid fractionation of barley leaf protoplasts</title><link>http://scien.net/enzyme/dehydrogenase/in-vivo-mitochondrial-pyruvate-dehydrogenase-activity-studied-by-rapid-fractionation-of-barley-leaf-protoplasts</link> <comments>http://scien.net/enzyme/dehydrogenase/in-vivo-mitochondrial-pyruvate-dehydrogenase-activity-studied-by-rapid-fractionation-of-barley-leaf-protoplasts#comments</comments> <pubDate>Sun, 19 May 2013 04:53:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[mncl]]></category> <category><![CDATA[pdcs]]></category> <category><![CDATA[photorespiratory]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/in-vivo-mitochondrial-pyruvate-dehydrogenase-activity-studied-by-rapid-fractionation-of-barley-leaf-protoplasts</guid> <description><![CDATA[Kroemer, Silke; Lernmark, Ulrika; Gardestrom, Per, 1994: In vivo mitochondrial pyruvate dehydrogenase activity, studied by rapid fractionation of barley leaf protoplasts. Journal Of Plant Physiology. 144(4-5): 485-490 Inactivation and activation of mitochondrial and chloroplastic pyruvate dehydrogenase (Pdh; Ec 1.2.4.1) have been studied in isolated organelles and protoplasts from barley leaves. The pyruvate dehydrogenase complex (Pdc) [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/in-vivo-mitochondrial-pyruvate-dehydrogenase-activity-studied-by-rapid-fractionation-of-barley-leaf-protoplasts/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>In vitro and in vivo temperature modulation of hepatic metabolism and DNA adduction of aflatoxin B1 in rainbow trout</title><link>http://scien.net/enzyme/dehydrogenase/in-vitro-and-in-vivo-temperature-modulation-of-hepatic-metabolism-and-dna-adduction-of-aflatoxin-b1-in-rainbow-trout</link> <comments>http://scien.net/enzyme/dehydrogenase/in-vitro-and-in-vivo-temperature-modulation-of-hepatic-metabolism-and-dna-adduction-of-aflatoxin-b1-in-rainbow-trout#comments</comments> <pubDate>Sun, 19 May 2013 04:29:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[adduction]]></category> <category><![CDATA[aflatoxicol]]></category> <category><![CDATA[nonshifted]]></category> <category><![CDATA[poikilotherms]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/in-vitro-and-in-vivo-temperature-modulation-of-hepatic-metabolism-and-dna-adduction-of-aflatoxin-b1-in-rainbow-trout</guid> <description><![CDATA[&#8220;Carpenter, Hillary M.; Zhang, Quan; El Zahr, Camille; Selivonchick, Daniel P.; Broch, Daniel E.; Curtis, Lawrence R., 1995: In vitro and in vivo temperature modulation of hepatic metabolism and DNA adduction of aflatoxin B1 in rainbow trout. Journal Of Biochemical Toxicology. 10(1): 1-10 Alterations in membrane lipid composition during temperature acclimation of poikilotherms is hypothesized [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/in-vitro-and-in-vivo-temperature-modulation-of-hepatic-metabolism-and-dna-adduction-of-aflatoxin-b1-in-rainbow-trout/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Impact of exercise intensity on body fatness and skeletal muscle metabolism</title><link>http://scien.net/enzyme/dehydrogenase/impact-of-exercise-intensity-on-body-fatness-and-skeletal-muscle-metabolism</link> <comments>http://scien.net/enzyme/dehydrogenase/impact-of-exercise-intensity-on-body-fatness-and-skeletal-muscle-metabolism#comments</comments> <pubDate>Sun, 19 May 2013 04:23:36 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[hadh]]></category> <category><![CDATA[hiit]]></category> <category><![CDATA[hydroxyacyl]]></category> <category><![CDATA[ninefold]]></category> <category><![CDATA[skinfolds]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/impact-of-exercise-intensity-on-body-fatness-and-skeletal-muscle-metabolism</guid> <description><![CDATA[Tremblay, Angelo; Simoneau, Jean Aime; Bouchard, Claude, 1994: Impact of exercise intensity on body fatness and skeletal muscle metabolism. Metabolism Clinical &#038; Experimental. 43(7): 814-818 The impact of two different modes of training on body fatness and skeletal muscle metabolism was investigated in young adults who were subjected to either a 20-week endurance-training (Et) program [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/impact-of-exercise-intensity-on-body-fatness-and-skeletal-muscle-metabolism/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>High-performance liquid chromatographic determination of dihydroorotate dehydrogenase of Plasmodium falciparum and effects of antimalarials on enzyme activity</title><link>http://scien.net/enzyme/dehydrogenase/high-performance-liquid-chromatographic-determination-of-dihydroorotate-dehydrogenase-of-plasmodium-falciparum-and-effects-of-antimalarials-on-enzyme-activity</link> <comments>http://scien.net/enzyme/dehydrogenase/high-performance-liquid-chromatographic-determination-of-dihydroorotate-dehydrogenase-of-plasmodium-falciparum-and-effects-of-antimalarials-on-enzyme-activity#comments</comments> <pubDate>Sun, 19 May 2013 04:00:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[dihydroorotate]]></category> <category><![CDATA[gametocyte]]></category> <category><![CDATA[menoctone]]></category> <category><![CDATA[primaquine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/high-performance-liquid-chromatographic-determination-of-dihydroorotate-dehydrogenase-of-plasmodium-falciparum-and-effects-of-antimalarials-on-enzyme-activity</guid> <description><![CDATA[Ittarat, Isra; Webster, H. Kyle; Yuthavong, Yongyuth, 1992: High-performance liquid chromatographic determination of dihydroorotate dehydrogenase of Plasmodium falciparum and effects of antimalarials on enzyme activity. Journal Of Chromatography Biomedical Applications. 582(1-2): 57-64 A reversed-phase high-performance liquid chromatographic technique for the determination of dihydroorotate dehydrogenase in Plasmodium falciparum was developed. The assay was applied to the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/high-performance-liquid-chromatographic-determination-of-dihydroorotate-dehydrogenase-of-plasmodium-falciparum-and-effects-of-antimalarials-on-enzyme-activity/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Herbicidal activity of an isopropylmalate dehydrogenase inhibitor</title><link>http://scien.net/enzyme/dehydrogenase/herbicidal-activity-of-an-isopropylmalate-dehydrogenase-inhibitor</link> <comments>http://scien.net/enzyme/dehydrogenase/herbicidal-activity-of-an-isopropylmalate-dehydrogenase-inhibitor#comments</comments> <pubDate>Sat, 18 May 2013 07:38:01 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[faberi]]></category> <category><![CDATA[ipmdh]]></category> <category><![CDATA[isobutenyl]]></category> <category><![CDATA[isopropylmalate]]></category> <category><![CDATA[ketoisocaproic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/herbicidal-activity-of-an-isopropylmalate-dehydrogenase-inhibitor</guid> <description><![CDATA[Wittenbach, Va; Teaney, Pw; Hanna, Ws; Rayner, D; Schloss, Jv, 1994: Herbicidal activity of an isopropylmalate dehydrogenase inhibitor. Plant physiology 106(1): 321-328 Isopropylmalate dehydrogenase (Ipmdh) is the third enzyme specific to leucine biosynthesis. It catalyzes the oxidative decarboxylation of 3-isopropylmalate (3-Ipm) to 2-ketoisocaproic acid. The partially purified enzyme from pea (Pisum sativum L.) shows a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/herbicidal-activity-of-an-isopropylmalate-dehydrogenase-inhibitor/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Glucose 6-phosphate dehydrogenase during cold-hardening in Lolium perenne</title><link>http://scien.net/enzyme/dehydrogenase/glucose-6-phosphate-dehydrogenase-during-cold-hardening-in-lolium-perenne</link> <comments>http://scien.net/enzyme/dehydrogenase/glucose-6-phosphate-dehydrogenase-during-cold-hardening-in-lolium-perenne#comments</comments> <pubDate>Sat, 18 May 2013 07:23:11 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[nonhardened]]></category> <category><![CDATA[yatsyn]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/glucose-6-phosphate-dehydrogenase-during-cold-hardening-in-lolium-perenne</guid> <description><![CDATA[Bredemeijer, G. M. M.; Esselink, G., 1995: Glucose 6-phosphate dehydrogenase during cold-hardening in Lolium perenne. Journal Of Plant Physiology. 145(4): 565-569 Glucose 6-phosphate dehydrogenase (G6pdh) was studied in crude and partially purified extracts from nonhardened and cold-hardened leaves of two cultivars of Lolium perenne L.: the winter hardy cv. Mondial and the less hardy cv. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/glucose-6-phosphate-dehydrogenase-during-cold-hardening-in-lolium-perenne/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Genetics and biochemistry of 1,2-dichloroethane degradation</title><link>http://scien.net/enzyme/dehydrogenase/genetics-and-biochemistry-of-12-dichloroethane-degradation</link> <comments>http://scien.net/enzyme/dehydrogenase/genetics-and-biochemistry-of-12-dichloroethane-degradation#comments</comments> <pubDate>Sat, 18 May 2013 07:17:08 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[chloroacetaldehyde]]></category> <category><![CDATA[chloroacetate]]></category> <category><![CDATA[chloroethanol]]></category> <category><![CDATA[dehalogenase]]></category> <category><![CDATA[dehalogenases]]></category> <category><![CDATA[dichloroethane]]></category> <category><![CDATA[haloacid]]></category> <category><![CDATA[haloalkane]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/genetics-and-biochemistry-of-12-dichloroethane-degradation</guid> <description><![CDATA[Janssen, Dick B.; Van Der Ploeg, Jan R.; Pries, Frens, 1994: Genetics and biochemistry of 1,2-dichloroethane degradation. Biodegradation. 5(3-4): 249-257 Dichloroethane (1,2-Dce) is a synthetic compound that is not known to be formed naturally. Nevertheless, several pure microbial cultures are able to use it as a sole carbon source for growth. Degradation of 1,2-Dce proceeds [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/genetics-and-biochemistry-of-12-dichloroethane-degradation/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Generation of a stable non-reverting Leu- mutant of Kluyveromyces lactis by gene disruption</title><link>http://scien.net/enzyme/dehydrogenase/generation-of-a-stable-non-reverting-leu-mutant-of-kluyveromyces-lactis-by-gene-disruption</link> <comments>http://scien.net/enzyme/dehydrogenase/generation-of-a-stable-non-reverting-leu-mutant-of-kluyveromyces-lactis-by-gene-disruption#comments</comments> <pubDate>Sat, 18 May 2013 07:08:41 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[isopropylmalate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/generation-of-a-stable-non-reverting-leu-mutant-of-kluyveromyces-lactis-by-gene-disruption</guid> <description><![CDATA[Meinhardt, F.; Holtwick, R., 1995: Generation of a stable non-reverting Leu- mutant of Kluyveromyces lactis by gene disruption. Applied Microbiology &#038; Biotechnology. 42(5): 734-737 The Leu2 gene coding for beta-isopropylmalate dehydrogenase of the yeast Kluyveromyces lactis strain Awj137 was disrupted. In the resulting Leu- strain a 0.57 times 10-3-base pairs PstI/BglII fragment of the Leu2 [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/generation-of-a-stable-non-reverting-leu-mutant-of-kluyveromyces-lactis-by-gene-disruption/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Gaba shunt in developing soybean seeds is associated with hypoxia</title><link>http://scien.net/enzyme/dehydrogenase/gaba-shunt-in-developing-soybean-seeds-is-associated-with-hypoxia</link> <comments>http://scien.net/enzyme/dehydrogenase/gaba-shunt-in-developing-soybean-seeds-is-associated-with-hypoxia#comments</comments> <pubDate>Sat, 18 May 2013 07:05:27 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[aminobutyrate]]></category> <category><![CDATA[glutamateoxaloacetate]]></category> <category><![CDATA[glutamatepyruvate]]></category> <category><![CDATA[nucellus]]></category> <category><![CDATA[semialdehyde]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/gaba-shunt-in-developing-soybean-seeds-is-associated-with-hypoxia</guid> <description><![CDATA[Shelp, Barry J.; Walton, Craig S.; Snedden, Wayne A.; Oresnik, Lucie G. Vv Tuinan J.; Layzell, David B., 1995: Gaba shunt in developing soybean seeds is associated with hypoxia. Physiologia Plantarum. 94(2): 219-228 In the present study we investigated the proposal that the gamma-aminobutyrate (Gaba) shunt in developing soybean (Glycine max (L.) Merr.) seeds is [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/gaba-shunt-in-developing-soybean-seeds-is-associated-with-hypoxia/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression of glutamate dehydrogenase and aspartate aminotransferase in eucalypt ectomycorrhizas</title><link>http://scien.net/enzyme/dehydrogenase/expression-of-glutamate-dehydrogenase-and-aspartate-aminotransferase-in-eucalypt-ectomycorrhizas</link> <comments>http://scien.net/enzyme/dehydrogenase/expression-of-glutamate-dehydrogenase-and-aspartate-aminotransferase-in-eucalypt-ectomycorrhizas#comments</comments> <pubDate>Sat, 18 May 2013 06:30:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[diversicolor]]></category> <category><![CDATA[ectomycorrhizas]]></category> <category><![CDATA[fagaceae]]></category> <category><![CDATA[gdhs]]></category> <category><![CDATA[hebeloma]]></category> <category><![CDATA[laccaria]]></category> <category><![CDATA[laccata]]></category> <category><![CDATA[pisolithus]]></category> <category><![CDATA[regnans]]></category> <category><![CDATA[urophylla]]></category> <category><![CDATA[westraliense]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/expression-of-glutamate-dehydrogenase-and-aspartate-aminotransferase-in-eucalypt-ectomycorrhizas</guid> <description><![CDATA[Botton, B.; Dell, B., 1994: Expression of glutamate dehydrogenase and aspartate aminotransferase in eucalypt ectomycorrhizas. New Phytologist. 126(2): 249-257 Previous studies of nitrogen-assimilating enzymes in ectomycorrhizal associations of the Pinaceae (Norway spruce, Douglas fir) and the Fagaceae (beech) have suggested that the host plant may regulate the expression of some fungal enzymes. To improve our [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/expression-of-glutamate-dehydrogenase-and-aspartate-aminotransferase-in-eucalypt-ectomycorrhizas/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Evidences of glyoxylate cycle in peroxisomes of senescent cotyledons</title><link>http://scien.net/enzyme/dehydrogenase/evidences-of-glyoxylate-cycle-in-peroxisomes-of-senescent-cotyledons</link> <comments>http://scien.net/enzyme/dehydrogenase/evidences-of-glyoxylate-cycle-in-peroxisomes-of-senescent-cotyledons#comments</comments> <pubDate>Sat, 18 May 2013 06:24:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[aconitase]]></category> <category><![CDATA[isocitric]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/evidences-of-glyoxylate-cycle-in-peroxisomes-of-senescent-cotyledons</guid> <description><![CDATA[Pistelli, Laura; De Bellis, Luigi; Alpi, Amedeo, 1995: Evidences of glyoxylate cycle in peroxisomes of senescent cotyledons. Plant Science (limerick). 109(1): 13-21 The metabolic pathway of the glyoxylate cycle has been investigated in peroxisomes isolated from senescent pumpkin (Cucurbita sp.) cotyledons. beta-oxidation activity, as well as activities of glyoxylate cycle enzymes isocitrate lyase (Ec 4.1.3.1), [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/evidences-of-glyoxylate-cycle-in-peroxisomes-of-senescent-cotyledons/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase</title><link>http://scien.net/enzyme/dehydrogenase/enzyme-enzyme-interaction-in-the-chloroplast-glyceraldehyde-3-phosphate-dehydrogenase-triose-phosphate-isomerase-and-aldolase</link> <comments>http://scien.net/enzyme/dehydrogenase/enzyme-enzyme-interaction-in-the-chloroplast-glyceraldehyde-3-phosphate-dehydrogenase-triose-phosphate-isomerase-and-aldolase#comments</comments> <pubDate>Sat, 18 May 2013 06:04:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enzyme-enzyme-interaction-in-the-chloroplast-glyceraldehyde-3-phosphate-dehydrogenase-triose-phosphate-isomerase-and-aldolase</guid> <description><![CDATA[Anderson, L. E.; Goldhaber Gordon, I. M.; Li, D.; Tang, X. Y.; Xiang, M.; Prakash, N., 1995: Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. Planta 196(2): 245-255 Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (Ec 1.2.1.13) and aldolase (Ec 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enzyme-enzyme-interaction-in-the-chloroplast-glyceraldehyde-3-phosphate-dehydrogenase-triose-phosphate-isomerase-and-aldolase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzyme sensors for the detection of pesticides</title><link>http://scien.net/enzyme/dehydrogenase/enzyme-sensors-for-the-detection-of-pesticides</link> <comments>http://scien.net/enzyme/dehydrogenase/enzyme-sensors-for-the-detection-of-pesticides#comments</comments> <pubDate>Sat, 18 May 2013 06:04:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[acetolactate]]></category> <category><![CDATA[sulfomethuron]]></category> <category><![CDATA[thifensulfuron]]></category> <category><![CDATA[thifensulfuronmethyl]]></category> <category><![CDATA[thiocholine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enzyme-sensors-for-the-detection-of-pesticides</guid> <description><![CDATA[Marty, J. L.; Mionetto, N.; Noguer, T.; Ortega, F.; Roux, C., 1993: Enzyme sensors for the detection of pesticides. Biosensors &#038; Bioelectronics. 8(6): 273-280 Various families of pesticides (insecticides, fungicides and herbicides) can be detected using enzymes. Organophosphorus and carbamate insecticides (e.g. paraoxon, methyl-parathion, aldicarb and carbofuran) inhibit acetylcholinesterase; dithiocarbamate fungicide (e.g. maneb) inhibits aldehyde [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enzyme-sensors-for-the-detection-of-pesticides/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzyme release by bovine neutrophils</title><link>http://scien.net/enzyme/dehydrogenase/enzyme-release-by-bovine-neutrophils</link> <comments>http://scien.net/enzyme/dehydrogenase/enzyme-release-by-bovine-neutrophils#comments</comments> <pubDate>Sat, 18 May 2013 06:04:04 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[opsonization]]></category> <category><![CDATA[pasteurellosis]]></category> <category><![CDATA[secretionrelease]]></category> <category><![CDATA[unopsonized]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enzyme-release-by-bovine-neutrophils</guid> <description><![CDATA[Watson, G. L.; Slocombe, R. F.; Robinson, N. E.; Sleight, S. D., 1995: Enzyme release by bovine neutrophils. American Journal Of Veterinary Research. 56(8): 1055-1061 Release of enzymes from cytoplasmic granules has been postulated to have a major role in neutrophil-mediated tissue injury. Secretion or release of primary granules, specific granules, and cytosolic enzymes by [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enzyme-release-by-bovine-neutrophils/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzyme activities related to glucose metabolism in Babesia microti and Babesia rodhaini</title><link>http://scien.net/enzyme/dehydrogenase/enzyme-activities-related-to-glucose-metabolism-in-babesia-microti-and-babesia-rodhaini</link> <comments>http://scien.net/enzyme/dehydrogenase/enzyme-activities-related-to-glucose-metabolism-in-babesia-microti-and-babesia-rodhaini#comments</comments> <pubDate>Sat, 18 May 2013 06:04:02 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[icdh]]></category> <category><![CDATA[iumg]]></category> <category><![CDATA[kgdh]]></category> <category><![CDATA[microti]]></category> <category><![CDATA[nmolmin]]></category> <category><![CDATA[rodhaini]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enzyme-activities-related-to-glucose-metabolism-in-babesia-microti-and-babesia-rodhaini</guid> <description><![CDATA[Shikano, Sojin; Shimada, Terumasa; Nakada, Ken Ichi; Hashiguchi, Rie; Ono, Kenichiro, 1995: Enzyme activities related to glucose metabolism in Babesia microti and Babesia rodhaini. Journal Of Veterinary Medical Science. 57(1): 93-97 A comparative study was carried out on the glucose metabolism in Babesia microti (Bm) and Babesia rodhaini (Br) by analyzing the enzyme activities. The [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enzyme-activities-related-to-glucose-metabolism-in-babesia-microti-and-babesia-rodhaini/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzymatic conversion of volatile metabolites in dry seeds during storage</title><link>http://scien.net/enzyme/dehydrogenase/enzymatic-conversion-of-volatile-metabolites-in-dry-seeds-during-storage</link> <comments>http://scien.net/enzyme/dehydrogenase/enzymatic-conversion-of-volatile-metabolites-in-dry-seeds-during-storage#comments</comments> <pubDate>Sat, 18 May 2013 06:03:54 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[cocklebur]]></category> <category><![CDATA[ethylacetate]]></category> <category><![CDATA[ethylformate]]></category> <category><![CDATA[ethylpropionate]]></category> <category><![CDATA[interconversions]]></category> <category><![CDATA[methoxyethanol]]></category> <category><![CDATA[methylacetate]]></category> <category><![CDATA[propanal]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enzymatic-conversion-of-volatile-metabolites-in-dry-seeds-during-storage</guid> <description><![CDATA[Zhang, Ming; Nakamaru, Yasuo; Tsuda, Sachiko; Nagashima, Tazuko; Esashi, Yohji, 1995: Enzymatic conversion of volatile metabolites in dry seeds during storage. Plant &#038; Cell Physiology. 36(1): 157-164 Dry seeds can transform volatile metabolites via enzymes pre-existing in them. The interconversion between acetaldehyde and ethanol occurred when they were applied gaseously to seeds of rice, lettuce, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enzymatic-conversion-of-volatile-metabolites-in-dry-seeds-during-storage/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enhancement of seed germination in high salinity by engineering mannitol expression in Arabidopsis thaliana</title><link>http://scien.net/enzyme/dehydrogenase/enhancement-of-seed-germination-in-high-salinity-by-engineering-mannitol-expression-in-arabidopsis-thaliana</link> <comments>http://scien.net/enzyme/dehydrogenase/enhancement-of-seed-germination-in-high-salinity-by-engineering-mannitol-expression-in-arabidopsis-thaliana#comments</comments> <pubDate>Sat, 18 May 2013 06:01:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[mtid]]></category> <category><![CDATA[mtld]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/enhancement-of-seed-germination-in-high-salinity-by-engineering-mannitol-expression-in-arabidopsis-thaliana</guid> <description><![CDATA[Thomas, J. C.; Sepahi, M.; Arendall, B.; Bohnert, H. J., 1995: Enhancement of seed germination in high salinity by engineering mannitol expression in Arabidopsis thaliana. Plant Cell &#038; Environment. 18(7): 801-806 The bacterial gene mtlD, which encodes mannitol 1-phosphate dehydrogenase (E.C.1.1.1.17), was transformed into Arabidopsis thaliana and expressed under control of the CaMV 35s promoter. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/enhancement-of-seed-germination-in-high-salinity-by-engineering-mannitol-expression-in-arabidopsis-thaliana/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Energy substrates for flight in the blister beetle Decapotoma lunata (Meloidae)</title><link>http://scien.net/enzyme/dehydrogenase/energy-substrates-for-flight-in-the-blister-beetle-decapotoma-lunata-meloidae</link> <comments>http://scien.net/enzyme/dehydrogenase/energy-substrates-for-flight-in-the-blister-beetle-decapotoma-lunata-meloidae#comments</comments> <pubDate>Sat, 18 May 2013 06:00:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[decapotoma]]></category> <category><![CDATA[hydroxyacyl]]></category> <category><![CDATA[meloidae]]></category> <category><![CDATA[oxidise]]></category> <category><![CDATA[pachnoda]]></category> <category><![CDATA[sinuata]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/energy-substrates-for-flight-in-the-blister-beetle-decapotoma-lunata-meloidae</guid> <description><![CDATA[Auerswald, L.; Gade, G., 1995: Energy substrates for flight in the blister beetle Decapotoma lunata (Meloidae). Journal of Experimental Biology 198(6): 1423-1431 We investigated the substrates for flight in the blister beetle Decapotoma lunata by (a) establishing the patterns of maximum activities of enzymes of various metabolic pathways in the flight muscles, (b) measuring the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/energy-substrates-for-flight-in-the-blister-beetle-decapotoma-lunata-meloidae/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of pesticides on soil enzymatic activities, Pratylenchus penetrans populations, black root rot, and growth of flue-cured tobacco</title><link>http://scien.net/enzyme/dehydrogenase/effects-of-pesticides-on-soil-enzymatic-activities-pratylenchus-penetrans-populations-black-root-rot-and-growth-of-flue-cured-tobacco</link> <comments>http://scien.net/enzyme/dehydrogenase/effects-of-pesticides-on-soil-enzymatic-activities-pratylenchus-penetrans-populations-black-root-rot-and-growth-of-flue-cured-tobacco#comments</comments> <pubDate>Fri, 17 May 2013 03:28:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[fenamiphos]]></category> <category><![CDATA[filip]]></category> <category><![CDATA[propamocarb]]></category> <category><![CDATA[stek]]></category> <category><![CDATA[telone]]></category> <category><![CDATA[vorlex]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effects-of-pesticides-on-soil-enzymatic-activities-pratylenchus-penetrans-populations-black-root-rot-and-growth-of-flue-cured-tobacco</guid> <description><![CDATA[Tu, C. M.; Marks, C. F.; Johnson, P. W.; Gayed, S. K.; Elliot, J. M., 1995: Effects of pesticides on soil enzymatic activities, Pratylenchus penetrans populations, black root rot, and growth of flue-cured tobacco. Journal Of Environmental Science &#038; Health Part B Pesticides Food Contaminants &#038; Agricultural Wastes. 30(2): 141-162 Field experiments were conducted on [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effects-of-pesticides-on-soil-enzymatic-activities-pratylenchus-penetrans-populations-black-root-rot-and-growth-of-flue-cured-tobacco/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of nematicides on populations of soil microflora and Pratylenchus penetrans, soil enzymes and flue-cured tobacco</title><link>http://scien.net/enzyme/dehydrogenase/effects-of-nematicides-on-populations-of-soil-microflora-and-pratylenchus-penetrans-soil-enzymes-and-flue-cured-tobacco</link> <comments>http://scien.net/enzyme/dehydrogenase/effects-of-nematicides-on-populations-of-soil-microflora-and-pratylenchus-penetrans-soil-enzymes-and-flue-cured-tobacco#comments</comments> <pubDate>Fri, 17 May 2013 03:26:21 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[dazomet]]></category> <category><![CDATA[fenamiphos]]></category> <category><![CDATA[telone]]></category> <category><![CDATA[vorlex]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effects-of-nematicides-on-populations-of-soil-microflora-and-pratylenchus-penetrans-soil-enzymes-and-flue-cured-tobacco</guid> <description><![CDATA[Tu, C. M.; Marks, C. F.; Johnson, P. W.; Elliot, J. M., 1995: Effects of nematicides on populations of soil microflora and Pratylenchus penetrans, soil enzymes and flue-cured tobacco. Journal Of Environmental Science &#038; Health Part B Pesticides Food Contaminants &#038; Agricultural Wastes. 30(1): 95-111 Field experiments were conducted on Fox loamy sand to study [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effects-of-nematicides-on-populations-of-soil-microflora-and-pratylenchus-penetrans-soil-enzymes-and-flue-cured-tobacco/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of high sucrose diet on insulin-like effects of vanadate in diabetic rats</title><link>http://scien.net/enzyme/dehydrogenase/effects-of-high-sucrose-diet-on-insulin-like-effects-of-vanadate-in-diabetic-rats</link> <comments>http://scien.net/enzyme/dehydrogenase/effects-of-high-sucrose-diet-on-insulin-like-effects-of-vanadate-in-diabetic-rats#comments</comments> <pubDate>Fri, 17 May 2013 03:22:06 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[hypoinsulinemia]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effects-of-high-sucrose-diet-on-insulin-like-effects-of-vanadate-in-diabetic-rats</guid> <description><![CDATA[Pugazhenthi, Subbiah; Angel, Joseph F.; Khandelwal, Ramji L., 1993: Effects of high sucrose diet on insulin-like effects of vanadate in diabetic rats. Molecular &#038; Cellular Biochemistry. 122(1): 77-84 The insulin-like effects of vanadate were compared in streptozotocin-induced diabetic rats fed on high starch control and high sucrose diets for a period of six weeks. Diabetic [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effects-of-high-sucrose-diet-on-insulin-like-effects-of-vanadate-in-diabetic-rats/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of some compounds on glutamine synthetase isoforms activity from triticale seedling leaves</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-some-compounds-on-glutamine-synthetase-isoforms-activity-from-triticale-seedling-leaves</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-some-compounds-on-glutamine-synthetase-isoforms-activity-from-triticale-seedling-leaves#comments</comments> <pubDate>Fri, 17 May 2013 03:01:02 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[hydrosulphide]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-some-compounds-on-glutamine-synthetase-isoforms-activity-from-triticale-seedling-leaves</guid> <description><![CDATA[Bielawski, Wieslaw, 1994: Effect of some compounds on glutamine synthetase isoforms activity from triticale seedling leaves. Acta Physiologiae Plantarum. 16(4): 303-308 The Mg-2+-dependent activity of the chloroplastic form of glutamine synthetase was activated by hydrosulphide compounds while the activity of the cytoplasmic form of the enzyme did not change under the same conditions. Moreover, the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-some-compounds-on-glutamine-synthetase-isoforms-activity-from-triticale-seedling-leaves/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of six promoter-intron combinations on transient reporter gene expression in einkorn, emmer and common wheat cells by particle bombardment</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-six-promoter-intron-combinations-on-transient-reporter-gene-expression-in-einkorn-emmer-and-common-wheat-cells-by-particle-bombardment</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-six-promoter-intron-combinations-on-transient-reporter-gene-expression-in-einkorn-emmer-and-common-wheat-cells-by-particle-bombardment#comments</comments> <pubDate>Fri, 17 May 2013 03:00:34 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[einkorn]]></category> <category><![CDATA[emmer]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-six-promoter-intron-combinations-on-transient-reporter-gene-expression-in-einkorn-emmer-and-common-wheat-cells-by-particle-bombardment</guid> <description><![CDATA[Takumi, Shigeo; Otani, Motoyasu; Shimada, Takiko, 1994: Effect of six promoter-intron combinations on transient reporter gene expression in einkorn, emmer and common wheat cells by particle bombardment. Plant Science (limerick). 103(2): 161-166 The effect of six promoter-intron combinations on transient expression of beta-glucuronidase (Gus) as the reporter gene was estimated in cultured einkorn (Triticum monococcum), [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-six-promoter-intron-combinations-on-transient-reporter-gene-expression-in-einkorn-emmer-and-common-wheat-cells-by-particle-bombardment/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of parathyroid hormone on osteoclasts in organ-cultured medullary bone</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-parathyroid-hormone-on-osteoclasts-in-organ-cultured-medullary-bone</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-parathyroid-hormone-on-osteoclasts-in-organ-cultured-medullary-bone#comments</comments> <pubDate>Fri, 17 May 2013 02:55:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-parathyroid-hormone-on-osteoclasts-in-organ-cultured-medullary-bone</guid> <description><![CDATA[Sugiyama, Toshie; Kusuhara, Seiji, 1994: Effect of parathyroid hormone on osteoclasts in organ-cultured medullary bone. Japanese Poultry Science. 31(6): 392-399 The enzyme activity and ultrastructure of osteoclasts in medullary bone cultured in the presence of parathyroid hormone (Pth) were examined using laying hens during the formative phase of the bone when an egg was in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-parathyroid-hormone-on-osteoclasts-in-organ-cultured-medullary-bone/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of five insecticides on microbial and enzymatic activities in sandy soil</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-five-insecticides-on-microbial-and-enzymatic-activities-in-sandy-soil</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-five-insecticides-on-microbial-and-enzymatic-activities-in-sandy-soil#comments</comments> <pubDate>Fri, 17 May 2013 02:45:35 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[amitraz]]></category> <category><![CDATA[aztec]]></category> <category><![CDATA[cyfluthrin]]></category> <category><![CDATA[formazan]]></category> <category><![CDATA[hgcl]]></category> <category><![CDATA[tebupirimphos]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-five-insecticides-on-microbial-and-enzymatic-activities-in-sandy-soil</guid> <description><![CDATA[Tu, C. M., 1995: Effect of five insecticides on microbial and enzymatic activities in sandy soil. Journal Of Environmental Science &#038; Health Part B Pesticides Food Contaminants &#038; Agricultural Wastes. 30(3): 289-306 A laboratory study was conducted to examine the effects of five insecticides on microbial and enzymatic activities important to fertility in sandy soil. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-five-insecticides-on-microbial-and-enzymatic-activities-in-sandy-soil/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of fenvalerate on protein and amino acid contents and enzyme activities in the ostracod Chrissia halyi</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-fenvalerate-on-protein-and-amino-acid-contents-and-enzyme-activities-in-the-ostracod-chrissia-halyi</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-fenvalerate-on-protein-and-amino-acid-contents-and-enzyme-activities-in-the-ostracod-chrissia-halyi#comments</comments> <pubDate>Fri, 17 May 2013 02:45:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[chrissia]]></category> <category><![CDATA[halyi]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-fenvalerate-on-protein-and-amino-acid-contents-and-enzyme-activities-in-the-ostracod-chrissia-halyi</guid> <description><![CDATA[Khan, Z; Khan, Ma, 1995: Effect of fenvalerate on protein and amino acid contents and enzyme activities in the ostracod Chrissia halyi. Pesticide science 45(3): 279-282 The short-term effect of fenvalerate on some metabolites and enzymes of protein metabolism in the ostracod Chrissia halyi was studied. The ostracods were subjected to two different concentrations of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-fenvalerate-on-protein-and-amino-acid-contents-and-enzyme-activities-in-the-ostracod-chrissia-halyi/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of 6-benzylaminopurine and thidiazuron on photosynthesis in crop plants</title><link>http://scien.net/enzyme/dehydrogenase/effect-of-6-benzylaminopurine-and-thidiazuron-on-photosynthesis-in-crop-plants</link> <comments>http://scien.net/enzyme/dehydrogenase/effect-of-6-benzylaminopurine-and-thidiazuron-on-photosynthesis-in-crop-plants#comments</comments> <pubDate>Fri, 17 May 2013 02:33:20 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category> <category><![CDATA[calvin]]></category> <category><![CDATA[phosphoribulokinase]]></category> <category><![CDATA[rubpc]]></category> <category><![CDATA[rubpco]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/effect-of-6-benzylaminopurine-and-thidiazuron-on-photosynthesis-in-crop-plants</guid> <description><![CDATA[Chernyad&#8217;ev, I. I., 1994: Effect of 6-benzylaminopurine and thidiazuron on photosynthesis in crop plants. Photosynthetica (prague). 30(2): 287-292 The effect of cytokinins benzylaminopurine (Bap) and thidiazuron on photosynthetic rate and enzyme activities in sugar beet, pea, meadow fescue and reed fescue leaves was studied. Low concentrations (3-10 g m-3) stimulated the net photosynthetic rate, the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/effect-of-6-benzylaminopurine-and-thidiazuron-on-photosynthesis-in-crop-plants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Dual role of free fatty acids in regulation of mitochondrial L-glycerol-3-phosphate dehydrogenase</title><link>http://scien.net/enzyme/dehydrogenase/dual-role-of-free-fatty-acids-in-regulation-of-mitochondrial-l-glycerol-3-phosphate-dehydrogenase</link> <comments>http://scien.net/enzyme/dehydrogenase/dual-role-of-free-fatty-acids-in-regulation-of-mitochondrial-l-glycerol-3-phosphate-dehydrogenase#comments</comments> <pubDate>Fri, 17 May 2013 02:25:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Dehydrogenase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/dehydrogenase/dual-role-of-free-fatty-acids-in-regulation-of-mitochondrial-l-glycerol-3-phosphate-dehydrogenase</guid> <description><![CDATA[Rauchova, Hana; Beleznai, Zsuzsa; Drahota, Zdenek, 1993: Dual role of free fatty acids in regulation of mitochondrial L-glycerol-3-phosphate dehydrogenase. Biochemistry &#038; Molecular Biology International. 30(1): 139-148 In brown adipose tissue mitochondria, the influence of free fatty acids on Fad-linked L-glycerol-3-phosphate dehydrogenase was investigated using either hydrophilic or hydrophobic electron acceptors. The apparent kinetic parameters were [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/dehydrogenase/dual-role-of-free-fatty-acids-in-regulation-of-mitochondrial-l-glycerol-3-phosphate-dehydrogenase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>