Sodium‐induced conformation changes in membrane transport proteins

FEBS Letters

Wheeler, Kenneth P.¹  Charalambous, Bambos M.¹ 

[1] School of Biological Sciences, University of Sussex, Brighton BN1 9QG, England

关键词: Membrane protein;    Sodium dependence;    Amino acid transport;   

DOI  :  10.1016/0014-5793(85)81016-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the presence of KC1, tryptic digestion of vesicles derived from pigeon erythrocyte membranes inactivates sodium-dependent uptake of alanine by the vesicles, whereas digestion in the presence of NaCl does not. Extensive degradation of vesicle proteins occurs under both conditions. Similarly, the extent of inhibition by N-ethylmaleimide of the sodium-dependent influxes of both glycine and alanine into human erythrocytes is greater when the cells are exposed to the thiol reagent in the presence of KC1 than when NaCl is used. These observations are interpreted as providing evidence for sodium-induced conformation changes in these transport proteins.

【 授权许可】

Unknown