An interpretation of human diaphorase isozymes in terms of three gene loci DIA1, DIA2 and DIA3
- 1 October 1977
- journal article
- research article
- Published by Wiley in Annals of Human Genetics
- Vol. 41 (2) , 139-149
- https://doi.org/10.1111/j.1469-1809.1977.tb01908.x
Abstract
SUMMARY: NADH and NADPH diaphorase isozymes have been studied in human tissues. Evidence from rare heterozygotes suggests that the red cell and main tissue forms of NADH diaphorase are products of the same locus DIA1 NADPH‐dependent diaphorase appears to be the product of a second locus DIA2 A third locus, DIA3 codes for the polymorphic sperm diaphorase. The products of this locus are also found in foetal tissues including placenta and adult brain and gonads. The products of these three loci may be distinguished by their substrate specificity, thermostability and molecular size.This publication has 24 references indexed in Scilit:
- Assignment of the DIA1 locus to chromosome 22Annals of Human Genetics, 1977
- The distribution of isoelectric points of human soluble proteins and in particular of the enzyme products of 88 human gene lociAnnals of Human Genetics, 1977
- Sperm Diaphorase: Genetic Polymorphism of a Sperm-Specific Enzyme in ManScience, 1976
- Generalised deficiency of cytochrome b5 reductase in congenital methaemoglobinaemia with mental retardationNature, 1975
- Further Data on the Incidence and Segregation of Genetically Determined Electrophoretic Variants of Human Red Cell NADH DiaphoraseHuman Heredity, 1975
- Presence of red cell type NADH-methemoglobin reductase (NADH-diaphorase) in human non erythroid cellsBiochemical and Biophysical Research Communications, 1972
- Thermostability studies on the isozymes of human phosphoglucomutaseAnnals of Human Genetics, 1970
- Genetically determined electrophoretic variants of human red cell NADH diaphoraseAnnals of Human Genetics, 1970
- Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemiaBiochemical and Biophysical Research Communications, 1967
- The enzymic defect of hereditary methemoglobinemia: diaphoraseBiochimica et Biophysica Acta, 1959