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pubmed:abstractText |
(1) Human erythrocyte membranes, when dialysed against water at pH 9.5, were partly solubilized, losing 80% of the membrane proteins and 65% of the membrane lipids. Sodium dodecyl sulphate gel electrophoresis of the particulate material revealed selective removal of proteins from the membrane. (2) The lipid-rich particulate material remaining retained the ability to bind specifically the nucleoside transport inhibitor, nitrobenzylthioinosine, previously shown to bind selectively to the nucleoside transport mechanism of whole erythrocytes and erythrocyte ghosts.
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