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Sodium‐induced conformation changes in membrane transport proteins
Author(s) -
Charalambous Bambos M.,
Wheeler Kenneth P.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81016-4
Subject(s) - chemistry , biophysics , sodium , membrane transport , membrane , membrane protein , biochemistry , biology , organic chemistry
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.