Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.41 (isocitrate dehydrogenase)
 3,101 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

"Null"-activity and low-activity variants for the liver supernatant isozymes of aldehyde oxidase (designated AOX-1 and AOX-2) were observed in inbred strains and in Harwell linkage testing stocks of Mus musculus. The genetic loci determining the activity of these isozymes (designated Aox-1 and Aox-2, respecitively) are closely linked on chromosome 1 near Id-1 (encoding the soluble isozyme of isocitrate dehydrogenase). Linkage data of Aox-1 with Id-1 and Dip-1 (encoding a kidney peptidase) demonstrated that this gene coincides with or is closely linked to Aox (Watson et al., 1972). Ontogenetic analyses demonstrated that liver AOX-1 appeared just before birth and increased in activity during postnatal development, whereas liver AOX-2 was observed only during postnatal development. Adult male livers exhibited higher AOX-1 and AOX-2 activities than adult female livers. Both isozymes were significantly reduced in activity by castration of adult males and increased following testosterone administration to castrated males and normal female mice.
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PMID:Genetics, ontogeny, and testosterone inducibility of aldehyde oxidase isozymes in the mouse: evidence for two genetic loci (Aox-I and Aox-2) closely linked on chromosome 1. 51 35

Electrophoretic and activity variants for the C2 isozyme of alcohol dehydrogenase (ADH-C2), the mitochondrial isozyme of aldehyde dehydrogenase (AHD-A2) and aldehyde oxidase isozymes (AOX-1; AOX-2) in inbred strains of Mus musculus were used to map the genes encoding these enzymes on the mouse genome. Adh-3 (encoding ADH-C2) was localized on chromosome 3 and was closely linked to a cis-acting regulator locus (Adh-3-t), which determined ADH-C2 activity in male reproductive tissues. Ahd-1 (encoding AHD-A2) was found on chromosome 4 near Gpd-1 (encoding the liver isozyme of glucose-6-phosphate dehydrogenase), whereas the aldehyde oxidase loci (Aox-1, Aox-2) were closely linked on chromosomes 1 near Id-1 (encoding isocitrate dehydrogenase).
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PMID:Genetic regulation of alcohol dehydrogenase, aldehyde dehydrogenase and aldehyde oxidase isozymes in the mouse. 699 77

Electrophoretic variation of enzymes in five Eimeria spp. of the domestic fowl, including nine strains, ten single-sporocyst clones and two single-sporozoite clones of E. acervulina, three strains each of E. maxima and E. tenella, two strains of E. praecox and one strain of E. necatrix, were assayed using cellulose acetate electrophoresis. Ten enzymes [aldehyde oxidase (AO), alkaline phosphatase (ALP), amylase (AMY), fumarate hydratase (FUM), glucose-6-phosphate dehydrogenase (G6PDH), glucose phosphate isomerase (GPI), glutamate-oxaloacetate transferase (GOT), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH) and phosphoglucomutase (PGM)] were analyzed for their ability to distinguish between these species and strains. Enzymatic activity of G6PDH, GPI, IDH, MDH and PGM was detected in all the Eimeria spp. examined. Strains within each species were characterized by the same electrophoretic variant of G6PDH. Electrophoretic variants of GPI and PGM were the most valuable in the identification of inter- and intra-specific variation, particularly in the field strains of E. acervulina and E. tenella. These two enzymes were used to examine single-sporocyst and single-sporozoite clones derived from two strains of E. acervulina. The enzymes in E. maxima appeared to be conserved, showing no variation among strains with the five enzymes detected. Relative mobilities, calculated as described in this paper, were found to be consistent between different electrophoresis runs and may serve as a reference when this medium is used.
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PMID:Isoenzymes of Eimeria from the domestic fowl: electrophoretic variants among species, strains and clones. 919 94