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Differences in the occurrence of glutathione transferase isoenzymes ec 2.5.1.18 in rat lung and liver


, : Differences in the occurrence of glutathione transferase isoenzymes ec 2.5.1.18 in rat lung and liver. Biochemical and Biophysical Research Communications 127(1): 80-86

Cytosolic GSH [glutathione] transferases were purified from rat lung by affinity chromatography followed by chromatofocusing. On the criteria of order of elution, substrate specificity, apparent subunit MW, sensitivity to inhibitors, and reaction with antibodies, transferase subunits equivalent to subunits 2, 3 and 4, in the binary combinations occurring in liver, were identified. However, subunit 1 (and therefore transferases 1-1 and 1-2) was not detected. The most conspicuous difference is the presence in lung of a new form, eluting at pH 8.7, which is not detected in rat liver. This isoenzyme (transferase pH 8.7) is characterized by its low apparent subunit MW and high efficiency in the conjugation of glutathione with anti-benzo(a)pyrene-7,8-dihydrodiol-9,10-epoxide, considered the ultimate carcinogen of benzo(a)-pyrene.

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