Inoue T, Yoshida Y, Isaka Y, Tagawa K
Department of Physiological Chemistry, Osaka University Medical School, Suita, Japan.
Biochem Biophys Res Commun. 1993 Feb 15;190(3):857-63. doi: 10.1006/bbrc.1993.1127.
Peptidyl-Prolyl cis-trans isomerase was isolated from bovine heart mitochondrial matrix. The enzyme has a M(r) of 19,000 and its activity was inhibited by cyclosporin A (inhibition constant, 6.9 nM), but not by FK-506. The mitochondrial content of the enzyme is in good agreement with the number of binding sites for cyclosporin A (85 pmol/mg of matrix protein). Partial amino acid sequencing showed that the enzyme has a serine-rich N-terminal extension and is similar to human cyclophilin 3 (Bergsma et al. (1991) J. Biol. Chem. 266, 23204-23214) rather than the cytosolic and endoplasmic reticulum isoforms. We conclude that this protein is mitochondrial cyclophilin and a homologue of human cyclophilin 3.
肽基脯氨酰顺反异构酶是从牛心脏线粒体基质中分离出来的。该酶的相对分子质量为19000，其活性受到环孢菌素A的抑制（抑制常数为6.9 nM），但不受FK-506的抑制。该酶在线粒体中的含量与环孢菌素A的结合位点数量（85 pmol/mg基质蛋白）高度一致。部分氨基酸序列分析表明，该酶具有富含丝氨酸的N端延伸，并且与人类亲环蛋白3相似（Bergsma等人，（1991年）《生物化学杂志》266，23204 - 23214），而不是与胞质和内质网同工型相似。我们得出结论，该蛋白质是线粒体亲环蛋白，也是人类亲环蛋白3的同源物。
