PURIFICATION AND CHARACTERIZATION OF E37, A MAJOR CHLOROPLAST ENVELOPE PROTEIN

被引：13

作者：

BLOCK, MA

JOYARD, J

DOUCE, R

机构：

[1] DBMS, PCV, UA no. 576 au CNRS

来源：

FEBS LETTERS | 1991年 / 287卷 / 1-2期

关键词：

CHLOROPLAST ENVELOPE; INNER ENVELOPE MEMBRANE; E37; POLYPEPTIDE; MEMBRANE PROTEIN PURIFICATION; AMINO ACID SEQUENCE; SPINACH CHLOROPLAST;

D O I：

10.1016/0014-5793(91)80042-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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).

引用

页码：167 / 170

页数：4

共 16 条

[1]

[Anonymous], METHODS CHLOROPLAST

[2]

BLOCK MA, 1983, J BIOL CHEM, V258, P3273

[3]

BLOCK MA, 1983, J BIOL CHEM, V258, P3281

[4] IDENTIFICATION AND PURIFICATION OF A DEREPRESSIBLE ALKALINE-PHOSPHATASE FROM ANACYSTIS-NIDULANS R2 [J].