Takahashi Y, Hirata Y, Burstein Y, Listowsky I
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461.
Biochem J. 1994 Dec 15;304 ( Pt 3)(Pt 3):849-52. doi: 10.1042/bj3040849.
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.
一种未知的30 kDa蛋白质经常与人谷胱甘肽S-转移酶从S-己基谷胱甘肽亲和基质中共同纯化出来。采用两步连续亲和色谱法从人肝脏标本中获得了该蛋白质的纯品。用无色杆菌蛋白酶I对该蛋白质进行消化,通过高效液相色谱法分离得到的肽段序列与大鼠线粒体δ3,δ2-烯酰辅酶A异构酶的序列高度同源。该人类蛋白质也以δ3-顺式辛烯酰辅酶A为底物表现出催化活性。因此,它被鉴定为肝脏δ3,δ2-烯酰辅酶A异构酶。