主要叶绿体被膜蛋白E37的纯化与特性分析

Purification and characterization of E37, a major chloroplast envelope protein.

作者信息

Block M A, Joyard J, Douce R

机构信息

DBMS/PCV, UA no. 576 au CNRS, CENG et UJF 85X, Grenoble, France.

出版信息

FEBS Lett. 1991 Aug 5;287(1-2):167-70. doi: 10.1016/0014-5793(91)80042-2.

DOI:10.1016/0014-5793(91)80042-2

PMID:1879527

Abstract

We have purified to homogeneity E37, the second major polypeptide of the inner membrane of the chloroplast envelope. The protein was retained on a Mono S column at pH 7, indicating it is a basic protein. After cyanogen cleavage, the protein was partially sequenced at 2 different sites. The sequence is compared with the deduced amino acid sequence of a cDNA coding for a 37 kDa envelope polypeptide recently published by Dreses-Werringloer et al. (Eur. J. Biochem. (1991) 195, 361-368.)

摘要

我们已将叶绿体被膜内膜的第二种主要多肽E37纯化至同质状态。该蛋白质在pH 7时保留在Mono S柱上，表明它是一种碱性蛋白质。经氰基裂解后，在两个不同位点对该蛋白质进行了部分测序。将该序列与Dreses-Werringloer等人最近发表的编码37 kDa被膜多肽的cDNA推导的氨基酸序列进行了比较。(《欧洲生物化学杂志》(1991年)195卷，361 - 368页。)