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Purification and Properties of Hamster Liver Ligandins, Glutathione S-Transferases¹

The Fels Research Institute and Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140

Glutathione S-transferases have been purified to homogeneity from Chinese hamster liver. Three enzyme forms were separated and designated Forms I, II, and III in order of their elution from carboxymethylcellulose columns. The forms exhibit close physical similarities to glutathione S-transferases B (ligandin) of rat liver and of human liver. However, enzyme kinetic analysis indicates that the hamster enzymes exhibit similar K_m values but higher V_max values towards common substrates compared with the rat and human forms. These differences, which explain the increased enzymic activities of hamster glutathione S-transferases in vivo and in vitro, appear to be related to slight differences in the peptide composition of hamster liver glutathione S-transferases compared to the rat and human enzymes.

¹ Supported by Research Grants AM-13531 and AM-08350 from the National Institute of Arthritis, Metabolism, and Digestive Diseases, by Grant HD-05874 from the National Institute of Child Health and Human Development, and by Grant CA-12227 to The Fels Research Institute from the National Cancer Institute.

² Ernest Cook Fellow of the Royal Society, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London, England.

³ To whom requests for reprints should be addressed.

Received 11/26/79. Accepted 2/26/80.

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