Purification and characterization of E37, a major chloroplast envelope protein

FEBS Letters

Block, Maryse A.¹  Joyard, Jacques¹  Douce, Roland¹ 

[1] DBMS/PCV, UA no. 576 au CNRS, CENG et UJF85X, F38041 Grenoble, France

关键词: Chloroplast envelope;    Inner envelope membrane;    E37 polypeptide;    Membrane protein purification;    Amino acid sequence;    Spinach chloroplast;    CAPS;    3-(cyclohexylamino)-1-propanesulfonic acid;   

DOI  :  10.1016/0014-5793(91)80042-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.)

【 授权许可】

Unknown