Effect of lipid fluidity upon the activity and structure of the 39 kDa porin from Enterobacter cloacae 908S

FEBS Letters

Ghosh, Robin¹  Aggeler, Robert¹ 

[1] Pharmaceutical Research Department, F. Hoffmann-La Roche and Co. Ltd, CH-4002 Basel, Switzerland

关键词: Membrane;    Membrane protein;    Reconstitution;    Fluorescence;    DTT;    dithiothreitol;    PMSF;    phenylmethylsulphonyl fluoride;    NaP;    sodium phosphate buffer;    O-POE;    octylpentaoxyethylene;    PAGE;    polyacrylamide gel electrophoresis;    DMPC;    dimyristoylphosphatidylcholine;    DOPC;    dioleoylphosphatidylcholine;    LPS;    lipopolysaccharide;    T c;    phase transition temperature;   

DOI  :  10.1016/0014-5793(87)80210-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 39 kDa porin from Enterobacter cloacae 908S was isolated in a lipopolysaccharide-free form using the non-ionic detergent, octylpentaoxyethylene, and reconstituted into vesicles of dimyristoylphosphatidylcholine (DMPC) and dioleoylphosphatidylcholine (DOPC), respectively. Porin activity, measured by the rate of hydrolysis of the lipid-impermeant β-lactam cephazoline by entrapped lactamase, could be demonstrated for porin-DMPC but not for porin-DOPC vesicles, and for the former was significantly lower in the gel than in the liquid-crystalline phase. The fluorescence changes are thought to arise from lipid phase-induced structural/dynamic changes of the porin structure.

【 授权许可】

Unknown