Does sphingomyelin inhibit the erythrocyte anion transport system?

FEBS Letters

Haase, Winfried¹  Schubert, Dieter¹  Scheuring, Uwe¹ 

[1] Max-Planck-Institut für Biophysik, Frankfurt am Main, FRG

关键词: Sphingomyelin;    Anion transport;    Band 3 protein;    Reconstitution;    (Erythrocyte membrane);    SPH;    sphingomyelin;    PC;    phosphatidylcholine;    H2DIDS;    4;    4′-diisothiocyanostilbene-2;    2′-disulfonate;   

DOI  :  10.1016/0014-5793(88)80738-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The anion transport protein of the human erythrocyte membrane, band 3, was incorporated into unilamellar sphingomyelin vesicles. The vesicles showed a rapid sulfate efflux which could be inhibited by specific inhibitors of the erythrocyte anion transport system. All band 3 molecules contributing to the inhibitor-sensitive flux component were arranged ‘right-side-out’. The turnover number of the transport protein for sulfate transport was virtually identical to that in phosphatidylcholine bilayers and around 6 times larger than in human erythrocyte membranes. Thus, in contrast to other claims, sphingomyelin does not inhibit the erythrocyte anion transport system.

【 授权许可】

Unknown