The subunit structure of a major glutathione S-transferase form, MT, in rat testis. Evidence for a heterodimer consisting of subunits with different isoelectric points

A major glutathione S ‐transferase form (pI 5.7) in rat testis (M T ) purified by S ‐hexyl‐glutathione affinity chromatography, followed by chromatofocusing, showed two polypeptide of pI 6.7 (Yn 1 ) and 6.0 (Yn 2 ), having apparently the same molecular mass of 26 kDa on two‐dimensional gel electrophoresis. Rechromatofocusing o the M T preparation after 4 M guanidine hydrochloride treatment revealed two additional protein peaks (pI 6.2 and 5.4)....