Abstract
1. 1. Red cell membranes were isolated from rhesus-monkey erythrocytes and their proteins were analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and compared to the membrane protein pattern of human red cells. 2. 2. Rhesus-monkey erythrocytes had a significantly different distribution of spectrin-binding proteins. Specifically, they lacked band 2.2, had relatively greater amounts of bands 2.3 and 4.2 and had less protein in band 4.1. 3. 3. Whereas band 3 in human red cell membranes is a wide and diffuse region, in the rhesus monkey it is a discrete and narrow band suggesting a greater degree of homogeneity. 4. 4. The low-molecular weight polypeptides; i.e. band 6—the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase—and bands 7–8, were significantly decreased in comparison to their human counterparts.
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