Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells
- 1 October 1986
- journal article
- research article
- Published by Springer Nature in Human Genetics
- Vol. 74 (2) , 174-175
- https://doi.org/10.1007/bf00282085
Abstract
The S-formylglutathione hydrolase (FGH) polymorphism of human red blood cells was studied in unrelated individuals, both by isoelectric focusing and starch gel electrophoresis, and with the substrates S-acetylglutathione and 4-methylumbelliferyl-acetate (the standard substrate for esterase D (ESD)). With both separation techniques the two substrates consistently gave similar and identically located zymograms. Thus, FGH (E.C.3.1.2.12) appears to be identical to ESD (E.C.3.1.1.1).This publication has 8 references indexed in Scilit:
- Genetic heterogeneity of S-formylglutathione hydrolaseAnnals of Human Genetics, 1986
- Genetic analysis of human lymphocyte proteins by two-dimensional gel electrophoresis:Human Genetics, 1984
- Polymorphism of Red Cell S-Formylglutathione Hydrolase in a Finnish PopulationHuman Heredity, 1984
- Electrophoretic Investigation of Formaldehyde Dehydrogenase from Human TissuesHuman Heredity, 1982
- The ESD polymorphism: Further studies of the ESD2 and ESD5 allele productsHuman Genetics, 1981
- [56] Thioesters of glutathionePublished by Elsevier ,1981
- Glutathione thiol esterases of human red blood cellsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Esterase D: a new human polymorphismAnnals of Human Genetics, 1973