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An unidentified 30 kDa protein frequently copurifies with human glutathione S-transferases from S-hexyl-glutathione affinity matrices. Application of two-step sequential affinity chromatographic methods yielded a homogeneous preparation of that protein from human liver specimens. The protein was digested with Achromobacter protease I, and sequences of peptides resolved by h.p.l.c. showed a high degree of identity with those of rat mitochondrial delta 3, delta 2-enoyl-CoA isomerase. The human protein also exhibited catalytic activity with delta 3-cis-octenyl CoA as a substrate. Thus it is identified as liver delta 3, delta 2-enoyl-CoA isomerase.

biochemical journal

Δ3, Δ2-enoyl-CoA isomerase is the protein that copurifies with human glutathione <i>S</i>-transferases from <i>S</i>-hexylglutathione affinity matrices

Δ3, Δ2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices