Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells

Hum Genet. 1986 Oct;74(2):174-5. doi: 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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carboxylesterase*
  • Carboxylic Ester Hydrolases / genetics*
  • Electrophoresis, Starch Gel
  • Erythrocytes / enzymology*
  • Humans
  • Isoelectric Focusing
  • Polymorphism, Genetic*
  • Thiolester Hydrolases / genetics*

Substances

  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • ESD protein, human
  • Thiolester Hydrolases
  • s-formylglutathione hydrolase