Glutathione S-transferases: Of rats and men

✍ Scribed by R. E. Kirsch; N. M. Bass

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 285 KB
• Volume: 6
• Category: Article
• ISSN: 0270-9139
• DOI: 10.1002/hep.1840060439

✦ Synopsis

Rat liver glutathione S-transferases have been puriried to apparent electrophoretic homogeneity by S-hexylglutathione-linked

Sepharose 6B affinity chromatography and CM-cellulose column chromatography. At least 1 1 transfer-activity peaks can be resolved including five Yb size homodimeric imzymes, two Y, size homodimeric imzymes, one Y, homodimeric isozyme, one Y, homodimeric isozyme, and two Y,-Y, heterdmeric imzymes. Distribution of the GSH peroxidase activity among the CM-cellulose column fractions suggests the existence of further multiplicity in this isozyme family. Substrate specificity patterns of the Yb subunit isozymes revealed a possibility that each of the five Yb-containing isozymes is composed of a different homodimeric Yb size subunit composition. Our findings on the increasing multiplicity of glutathione S-transfer-isozymes are consistent with the notion that multiple iso- zymes of overlapping substrate specificities are required to detoxify a multitude of xenobiotics in addition to serving other important physiological functions.