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)

Proximal tubules were isolated in highly pure form from rabbit cortices by a mechanical procedure that is known to preserve the structural and metabolic aspects of the tubular cells. Postnuclear supernates prepared from the isolated tubules were subjects to isopycnic centrifugation in linear sucrose gradients. The enzyme activities associated with the plasma membrane (gamma-glutamyl transpeptidase, amino-peptidase M, alkaline phosphatase, Na-K-ATPase, and phosphodiesterase I) exhibited sharp unimodal frequency-density profiles with a median density near 1.16 g/ml, which shifted to a heavier density when treated with digitonin. The lysosomal enzymes, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and cathepsin B, and the peroxisomal enzyme catalase exhibited particle-associated activity near a density of 1.22 g/ml. Disruption of these particles by freezing and thawing resulted in these activities appearing in the rho = 1.10 g/ml region of the gradient where the soluble cytosolic enzyme, phosphoglucomutase, exhibited activity. Cytochrome oxidase activity typical of mitochondria gave a sharp unimodal profile at rho = 1.18 g/ml. Microsomal glucose-6-phosphatase and NADPH: cytochrome c reductase activities gave median densities near 1.16 g/ml, which did not change after incubation with digitonin. Galactosyl transferase activity gave a skewed profile at rho = 1.16 g/ml and showed a slight shift to heavier density after digitonin. This study of the enzymatic activities and density gradient distribution of the components of the proximal tubule cells provides the methodology for the further study of the cellular processing of endogenous and exogenous substances by this vital cell type.
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PMID:Analytical cell fractionation of isolated rabbit renal proximal tubules. 730 Jan 16

Several mitochondrial genes from a large number of different fungi, mammals and plants have been sequenced but little is known about the corresponding translation products. We have affinity purified cytochrome c reductase from potato mitochondria and isolated the mitochondrially encoded cytochrome b protein. Amino-terminal sequencing reveals that the polypeptide does not start with a methionine. Comparison of the amino acid sequence with the recently published sequence of the gene encoding the cytochrome b apoprotein suggests that the N-formylmethionine is removed. This result provides the first evidence for the presence of a deformylase and a methionine aminopeptidase in mitochondria.
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PMID:Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein. 842 Jul 97