DISULFIDE-LINKED PEPTIDES IN THE CHLOROPLAST THYLAKOID MEMBRANE

被引：6

作者：

ANDERSON, LE

MANABE, K

机构：

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 579卷 / 01期

基金：

美国国家科学基金会;

关键词：

(Thylakoid membrane); Disulfide bond; Peptide dimer;

D O I：

10.1016/0005-2795(79)90081-3

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：

Two peptides move out from the diagnonal when dodecyl sulfate gels of pea leaf chloroplast thylakoid membrane proteins are treated with a reducing agent and electrophoresed in the second dimension. Apparently two of the proteins in the thylakoid membrane are disulfide linked dimers. Additional changes in the electrophoretic mobility of certain peptides occur when thylakoid membranes are denatured in the presence of reducing agents: these peptides probably contain intrapeptide disulfide bonds or prosthetic groups covalently attached to the peptide through disulfide bonds. © 1979.

引用

页码：1 / 9

页数：9

共 12 条

[1] LIGHT MODULATION OF ENZYME-ACTIVITY IN CHLOROPLASTS - GENERATION OF MEMBRANE-BOUND VICINAL-DITHIOL GROUPS BY PHOTOSYNTHETIC ELECTRON-TRANSPORT [J].