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)

By means of starch electrophoresis, 52 proteins and enzymes of Microtus arvalis and M. subarvalis were studied to establish the extent of their similarity. Out of 52 markers studied, 7 proteins and enzymes had different electrophoretic mobility: glucose-6-phosphate dehydrogenase (G6PD), phosphogluconate dehydrogenase (PGD), diaphorase (DP), adenylate kinase (AK), lactate dehydrogenase B (LDHB), alpha-galactosidase (GAL) and hemoglobin (Hb), which make up to 13% of all the enzymes and proteins studied. The differences found between the two species studied by electrophoretic mobility of G6PD, AK, GAL and Hb, as well as the absence of intraspecific polymorphism for the above proteins permit to consider these proteins as species-specific markers, with the help of which M. arvalis and M. subarvalis can be distinguished. It should be emphasized that intraspecific polymorphism was found for PGD, LDHB and DP in M. arvalis, while in M. subarvalis these proteins were monomorphic and identical, in their electrophoretic mobility, to one of electrophoretic variants of M. arvalis. Therefore, only one of allelic variants of PGD, LDHB and DP is species-specific. Estimation of the extent of genetic similarity based on analysis of distribution of gene frequencies for polymorphic loci of M. arvalis and M. subarvalis by means of Nei's method gave the value of 0.312, the genetic distance being 1.164. The data obtained, together with the known cytogenetic data, point to a species rank of the species studied. Moreover, in spite of the morphological similarity between M. arvalis and M. subarvalis, the estimation of genetic similarity proved to be close to that for morphologically contrasting species.
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PMID:[Evaluation of the degree of genetic divergence in the twin species of the common vole Microtus arvalis and Microtus subarvalis (Rodentia)]. 638 3

The electrophoretic mobilities of 52 enzymes and proteins were used as measures of the genetic similarity between the sibling species Microtus arvalis and M. subarvalis. The two vole species differed in the electrophoretic mobilities of seven (glucose-6-phosphate dehydrogenase, adenylate kinase, diaphorase, lactate dehydrogenase-A, alpha-galactosidase, 6-phosphogluconate dehydrogenase, and hemoglobin) of these markers. This allowed us to accept the seven markers assayed as species-specific markers. Based on the frequency distribution of the genes at the polymorphic loci of M. arvalis and M. subarvalis, the degree of their genetic similarity was estimated as 0.312 and the genetic distance as 1.164 by Nei's formula. The estimates for genetic similarity were close to those obtained for species recognized as distinct.
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PMID:An estimation of the degree of the genetic divergence of sibling species Microtus arvalis and Microtus subarvalis (Rodentia) based on electrophoretic analysis. 639 94

Subcellular localization of hexokinase in the honeybee drone retina was examined following fractionation of cell homogenate using differential centrifugation. Nearly all hexokinase activity was found in the cytosolic fraction, following a similar distribution as the cytosolic enzymatic marker, phosphoglycerate kinase. The distribution of enzymatic markers of mitochondria (succinate dehydrogenase, rotenone-insensitive cytochrome c reductase, and adenylate kinase) indicated that the outer mitochondrial membrane was partly damaged, but their distributions were different from that of hexokinase. The activity of hexokinase in purified suspensions of cells was fivefold higher in glial cells than in photoreceptors. This result is consistent with the hypothesis based on quantitative 2-deoxy[3H]glucose autoradiography that only glial cells phosphorylate significant amounts of glucose to glucose-6-phosphate. The activities of alanine aminotransferase and to a lesser extent of glutamate dehydrogenase were higher in the cytosolic than in the mitochondrial fraction. This important cytosolic activity of glutamate dehydrogenase was consistent with the higher activity found in mitochondria-poor glial cells. In conclusion, this distribution of enzymes is consistent with the model of metabolic interactions between glial and photoreceptor cells in the intact bee retina.
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PMID:Cellular and subcellular localization of hexokinase, glutamate dehydrogenase, and alanine aminotransferase in the honeybee drone retina. 815 42

1. Mitochondria isolated from rat liver were disrupted with 0.3 per cent deoxycholate and a number of subfractions were isolated from this preparation by differential centrifugation. 2. The protein N, RNA and phospholipide content, as well as the succinoxidase, cytochrome c oxidase, adenylate kinase, and DPNH-cytochrome c reductase of these fractions were determined. 3. Two of these subfractions, found to consist of mitochondrial membranes (2), contained approximately 12 per cent of the protein N and approximately 35 per cent of the phospholipide of the whole mitochondria and accounted for approximately 70 per cent of the succinoxidase and cytochrome c oxidase activity of the original mitochondrial preparation. There was no discernible adenylate kinase, DPNH-cytochrome c reductase, or phosphorylating activities in these fractions, nor could they oxidize other substrates of the Krebs's cycle. 4. The most active fraction (60 minutes at 105,000 g pellet) had a higher phospholipide/protein value than the whole mitochondria and showed a seven-to elevenfold concentration of succinoxidase and cytochrome c oxidase activities. 5. Evidence has been given to indicate that the various components of the succinoxidase complex are present in this membrane fraction in the same relative proportions as in the whole mitochondria. 6. The implications of these findings are discussed.
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PMID:Cytochemical studies of mitochondria. II. Enzymes associated with a mitochondrial membrane fraction. 1339 36

Although Duchenne muscular dystrophy is primarily classified as a neuromuscular disease, cardiac complications play an important role in the course of this X-linked inherited disorder. The pathobiochemical steps causing a progressive decline in the dystrophic heart are not well understood. We therefore carried out a fluorescence difference in-gel electrophoretic analysis of 9-month-old dystrophin-deficient versus age-matched normal heart, using the established MDX mouse model of muscular dystrophy-related cardiomyopathy. Out of 2,509 detectable protein spots, 79 2D-spots showed a drastic differential expression pattern, with the concentration of 3 proteins being increased, including nucleoside diphosphate kinase and lamin-A/C, and of 26 protein species being decreased, including ATP synthase, fatty acid binding-protein, isocitrate dehydrogenase, NADH dehydrogenase, porin, peroxiredoxin, adenylate kinase, tropomyosin, actin, and myosin light chains. Hence, the lack of cardiac dystrophin appears to trigger a generally perturbed protein expression pattern in the MDX heart, affecting especially energy metabolism and contractile proteins.
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PMID:Proteomic Profiling of the Dystrophin-Deficient MDX Heart Reveals Drastically Altered Levels of Key Metabolic and Contractile Proteins. 2050 50


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