Sodium-induced conformation changes in membrane transport proteins.
In the presence of KCl, 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 KCl than when NaCl is used. These observations are interpreted as providing evidence for sodium-induced conformation changes in these transport proteins.
D000409:Alanine / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active; D010856:Columbidae; D004910:Erythrocyte Membrane / Q000032:analysis / Q000187:drug effects; D005033:Ethylmaleimide / Q000494:pharmacology; D005998:Glycine / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis*; D011487:Protein Conformation / Q000187:drug effects; D012964:Sodium / Q000494:pharmacology*
D000596:Amino Acids; D008565:Membrane Proteins; D012964:Sodium; D005033:Ethylmaleimide; D000409:Alanine; D005998:Glycine