DIFFERENCES IN RED-CELL MEMBRANE-PROTEINS IN RHESUS-MONKEY ERYTHROCYTES

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. 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. 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. The low MW 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.