Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A comparative study of 27 enzymes and proteins in blue and silver foxes was carried out by means of starch gel electrophoresis. The structure of these enzymes and proteins is determined by about 33 genes. It is shown that a number of blood enzymes and proteins of these species is represented by a single electrophoretic form, while lactate dehydrogenase, carboanhydrase, arylesterase, carboxylesterase, diaphorase, hexokinase and tetrasolium oxidase have several forms. It is also found that these species differ in seven enzymes and proteins: diaphorase, G-6-PD, adenylate kinase, carboxylesterase, albumin, prealbumin, transferrins. Other enzymes and proteins are similar in their electrophoretic mobility. The data obtained afford the evidence that the two species (Vulpes vulpes and Alopex lagopus) differ in a set of enzymes and proteins.
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PMID:[Homologous gene expression in intergeneric fox hybrids (Alopex lagopus x Vulpes vulpes). I. Comparative electrophoretic analysis of blood proteins and enzymes in Arctic and silver foxes]. 121 28

A genetically linked marker locus is sought for the Booroola gene (FecB), a major gene which confers increased prolificacy in sheep. We examined 18 polymorphic proteins in sheep and found 10 to be informative in half-sib families where the Booroola gene was segregating. Recombination was observed between each of the protein loci and the Booroola gene. The loci and exclusion distance for each (calculated as the recombination fraction where the lod score was equal to -2.0) are as follows: NADH diaphorase, DIA1 (9.2 cM); arylesterase, EsA (11.9 cM); haemoglobin beta chain, HBB (17.5 cM); leucine amino peptidase, LAP (19.7 cM); malic enzyme, ME1 (14.8 cM); ovine plasminogen antigen, OPA (12.6 cM); alpha-1-protease inhibitor, PI2 (5.7 cM), erythrocyte 'X' protein, Prot-X (25.3 cM); post transferrin, PTF (2.2 cM); transferrin, TF (33.8 cM).
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PMID:Genetic linkage analysis between protein polymorphisms and the FecB major gene in sheep. 141 47

1. After conventional fractionation of rat liver homogenates in 0.88m-sucrose the mitochondrial fraction was subjected to short-term water lysis followed by separation of the resulting membrane preparations. 2. Phosphatidate formation was measured in all subcellular fractions and subfractions and was compared with the distribution of succinate dehydrogenase, monoamine oxidase, rotenone-insensitive NADH cytochrome c reductase, arylsulphatase, urate oxidase, arylesterase and glucose 6-phosphatase. 3. The results obtained indicated that mitochondria were capable of synthesizing phosphatidate, though this activity was only about one-third of the total homogenate activity. 4. Mitochondrial phosphatidate formation was located predominantly in the outer mitochondrial membrane. Although this membrane preparation was found to be significantly contaminated by the microsomal fraction, this contamination was estimated to account for not more than about 20% of the total phosphatidate formation observed in preparations of outer mitochondrial membrane.
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PMID:Phosphatidate biosynthesis in mitochondrial subfractions of rat liver. 430 22

The subcellular localization of the omega-hydroxylase of Saccharomycopsis lipolytica was assessed by the analytical fractionation technique, originally described by de Duve C., Pressman, B.C., Gianetto, R., Wattiaux, R. and Appelmans, F., and hitherto little, if at all, applied to yeasts. Protoplasts were separated in six fractions by differential centrifugation. Some of these fractions were further fractionated by density gradient centrifugation. The distribution of omega-hydroxylase and 15 other constituents chosen as possible markers of its subcellular entities. (1) Mitochondria were characterized by particulate malate dehydrogenase, particulate Antimycin A-insensitive NADH-cytochrome c reductase, oligomycin-sensitive and K+-stimulated ATPase pH 9. (2) Most if not all of the catalase and urate oxidase is peroxisomal. (3) Free ribosomes account for most RNA. (4) Nucleoside diphosphatase is for the first time reported in a yeast and appears to belong to an homogeneous population of small membranes. (5) The soluble compartment contains magnesium pyrophosphatase, alkaline, 5'-nucleotidase and part of the NADH-cytochrome c reductase. Latent arylesterase and ATPase pH 7 have an unspecific distribution. Alkaline phosphodiesterase I has not been detected.
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PMID:Subcellular distribution of enzymes in the yeast saccharomycopsis lipolytica, grown on n-hexadecane, with special reference to the omega-hydroxylase. 626 2

A comparison was made of the properties of microsomes prepared from the small intestines of guinea pigs and rats. The NADPH2 cytochrome c reductase activity and cytochrome b5 and cytochrome P-450 content in rat microsomes was 42, 47 and 64% of that in the guinea pig, ethoxycoumarin deethylase activity was comparable, while arylesterase activity was twice as active in rats as guinea pigs. Investigation of the distribution of these and other parameters in rat intestinal epithelia revealed a preferential location of cytochrome P-450 in the villous tip while other parameters showed a more similar distribution between microsomes prepared from the villous tip and crypt.
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PMID:Intestinal microsomal drug metabolism. A comparison of rat and guinea-pig enzymes, and of rat crypt and villous tip cell enzymes. 2104 39