Selective solubilization of chlorosome proteins in Chloroflexus aurantiacus

FEBS Letters

Zuber, Herbert¹  Frank, Gerhard¹  Brunisholz, René¹  Eckhardt, Anne¹ 

[1] Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

关键词: Chlorosome;    c-Protein;    BChlc-binding polypeptide;    Chloroflexus aurantiacus;    BChlc;    bacteriochlorophyll c;   

DOI  :  10.1016/0014-5793(90)80924-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown