SELECTIVE SOLUBILIZATION OF CHLOROSOME PROTEINS IN CHLOROFLEXUS-AURANTIACUS

被引：11

作者：

ECKHARDT, A

BRUNISHOLZ, R

FRANK, G

ZUBER, H

机构：

[1] Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg

来源：

FEBS LETTERS | 1990年 / 267卷 / 02期

关键词：

BChlc-binding polypeptide; c-Protein; Chloroflexus aurantiacus; Chlorosome;

D O I：

10.1016/0014-5793(90)80924-8

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：

Proteins were solubilized selectively from chlorosomes of Chloroflexus aurantiacus by electrophoretic gel filtration according to Griebenow et al. Whereas the 11 kDa and 18 kDa proteins were extracted almost completely, the remaining modified chlorosomes contained high amounts of pigment and c-protein. It was concluded that the c-protein in contradiction to the publication by Griebenow et al. is indeed localized in the interior of Chloroflexus chlorosomes. © 1990.

引用

页码：199 / 202

页数：4

共 12 条

[11] VISUALIZATION OF THE SUPRAMOLECULAR ARCHITECTURE OF CHLOROSOMES (CHLOROBIUM TYPE VESICLES) IN FREEZE-FRACTURED CELLS OF CHLOROFLEXUS-AURANTIACUS [J].