Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analyses of DIA4 activity in cultured cells from a random population, a small family and human/rodent somatic cell hybrids support the view that the quantitative polymorphism of human DIA4 can be attributed to the segregation of a 'low activity' allele. (1) In a series of lymphoblastoid cell lines from 52 unrelated individuals, three lines were found which did not exhibit DIA4 after electrophoresis and showed low levels of NADPH diaphorase activity. The frequency (6%) of the DIA4 'absent' phenotype is close to that (4%) determined previously by analysis of post-mortem tissue. (2) Cultured fibroblasts from a small family in which the DIA 4 low-activity allele was apparently segregating were analysed. The NADPH diaphorase activity of the propositus (DIA4 'absent' phenotype) was very low (less than 6% of normal). He also exhibited very weak DIA4 isozymes of unusual electrophoretic mobility. The activity of both parents and sib was about half the normal level, suggesting that these individuals are heterozygous for the low-activity allele. (3) Analysis of a series of independent human/hamster hybrid clones, made using a human parent heterozygous for phosphoglycolate phosphatase (PGP) and DIA4, suggested that in this particular individual the DIA 4 low-activity allele segregates with the PGP 2 allele. However, there were 2 hybrids amongst a total of 16 which gave discordant results and these are to be the subject of further analysis by subcloning.
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PMID:A genetic characterization of the human diaphorase-4 deficiency. 630 68

A human FAD-dependent diaphorase, DIA4, has been studied in 29 independent human-rodent hybrids and in 17 subclones. The results suggest that the locus DIA4 is on chromosome 16.
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PMID:Assignment of a human diaphorase (DIA4) to chromosome 16. 689 12

A diaphorase (DIA4), different from similar enzymes so far described in man, has been detected electrophoretically in human tissues and fibroblasts. The enzyme which is active both with NADH and NADPH was missing in erythrocytes. It was consistently undetectable in part of the diploid fibroblast cultures analyzed. The activity could be separated by Cellogel electrophoresis from rodent diaphorases. In manmouse somatic cell hybrids human DIA4 segregated with chromosome 16. This result indicates that its structural gene is located on this autosome. The enzyme exhibits similarities with a NAD(P)H dehydrogenase (EC 1.6.99.2) described in rat liver.
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PMID:Assignment of a structural gene for a fourth human diaphorase (DIA4) to chromosome 16 in man-mouse somatic cell hybrids. 692 11

A newly discovered human diaphorase, designated diaphorase-4, which accounts for a major part of the diaphorase activity of most tissues but does not occur in erythrocytes, is described. In contrast with other human diaphorases, it is dependent on FAD for activity after electrophoresis, inhibited by low concentrations of dicoumarol and shows a marked affinity for Cibacron Blue. The molecular weight was estimated to be 49000 +/- 1800 by gel filtration. Diaphorase-4 appears to show person-to-person quantitative variation, so that about 4% of the population lack appreciable enzyme activity, but it is not yet clear whether this variation is of genetic or non-genetic origin.
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PMID:Human FAD-dependent NAD(P)H diaphorase. 739 57