Abstract
Human erythrocytes were treated with pronase under conditions which gave complete cleavage of the pronase-sensitive major protein and glycoprotein components of the membrane. 86Rb + influx of these modified cells did not differ significantly from that of untreated cells, and showed identical sensitivity to inhibition by ouabain. Pronase treatment of porous erythrocyte ghost membranes resulted in complete loss of (Na + + K +)-ATPase activity. These results indicate that the cation-transport complex is not readily accessible from the outer surface of native intact membranes.
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