芳香化酶细胞色素P-450。从人胎盘中纯化及鉴定该酶。

Aromatase cytochrome P-450. Purification and characterization of the enzyme from human placenta.

作者信息

Vickery L E, Kellis J T

机构信息

Department of Physiology and Biophysics, University of California, Irvine 92717.

出版信息

Steroids. 1987 Jul-Sep;50(1-3):29-36. doi: 10.1016/0039-128x(83)90059-4.

DOI:10.1016/0039-128x(83)90059-4

PMID:3504064

Abstract

Aromatase cytochrome P-450 (P-450arom) was purified from human placental microsomes. Preparations exhibit a single major band of approximately 55 kDa on SDS-polyacrylamide gel electrophoresis and have a specific content of 11-13 nmol P-450/mg protein. The purified enzyme exhibits spectral properties typical of ferric and ferrous forms of cytochromes P-450. Full enzymatic activity can be reconstituted with rabbit liver P-450 reductase, and catalytic characteristics similar to aromatase in microsomes are observed. Rabbit antibodies to purified P-450arom were affinity purified and show high specificity and sensitivity on immunoblots.

摘要

芳香化酶细胞色素P-450（P-450arom）从人胎盘微粒体中纯化得到。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上，制剂呈现出一条约55 kDa的主要条带，且每毫克蛋白质中细胞色素P-450的含量为11 - 13 nmol。纯化后的酶表现出细胞色素P-450铁离子和亚铁离子形式的典型光谱特性。完整的酶活性可以用兔肝P-450还原酶重建，并且观察到其催化特性与微粒体中的芳香化酶相似。针对纯化后的P-450arom制备的兔抗体经过亲和纯化，在免疫印迹上显示出高特异性和高灵敏度。