title: Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells.
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).
mesh_terms: D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000235:genetics*; D004592:Electrophoresis, Starch Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007525:Isoelectric Focusing; D011110:Polymorphism, Genetic; D013869:Thiolester Hydrolases / Q000235:genetics*
chemical_list: D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; C020118:ESD protein, human; D013869:Thiolester Hydrolases; C020149:s-formylglutathione hydrolase