未成熟大鼠中雌激素诱导的子宫蛋白（IP）——肌酸激酶的纯化与特性鉴定

Purification and characterization of creatine kinase, an estrogen-induced uterine protein (IP) from immature rats.

作者信息

Kumar S A, O'Connor D L, Seeger J I, Beach T A, Dickerman H W

出版信息

Biochem Biophys Res Commun. 1983 Feb 28;111(1):156-65. doi: 10.1016/s0006-291x(83)80130-2.

Abstract

An estrogen-responsive translational product, the induced protein (IP) first described by Notides and Gorski (8), was obtained solely from the target organ, immature rat uterus, and purified to homogeneity in a procedure using two chromatography steps. The purified IP has a molecular weight of 49,000, and the isoelectric point is 5.2. Creatine kinase activity is associated with the homogeneous IP. There are some differences between the uterine enzyme and the creatine kinase BB isoenzyme, including differences in stability, and sensitivity to mercaptans. Estrogen-induced creatine kinase purified by this simple, reproducible method is a useful antigen for further studies on the translation and transcription processes involved in hormone-modulated synthesis.

摘要

一种雌激素反应性翻译产物，即最初由诺蒂德斯和戈尔斯基（8）描述的诱导蛋白（IP），仅从靶器官——未成熟大鼠子宫中获得，并通过两步色谱法纯化至均一。纯化后的IP分子量为49000，等电点为5.2。肌酸激酶活性与均一的IP相关。子宫酶与肌酸激酶BB同工酶之间存在一些差异，包括稳定性和对硫醇的敏感性方面的差异。通过这种简单、可重复的方法纯化的雌激素诱导型肌酸激酶是用于进一步研究激素调节合成所涉及的翻译和转录过程的有用抗原。