Abstract
Reports of considerable species differences in the mammalian erythrocyte membrane glycoprotein composition led us to conduct a preliminary investigation of the platelet membrane glycoprotein composition in a range of mammals (15 species). Electrophoretic studies of detergent solubilized membranes and protease released acidic glycopeptides suggest considerable species differences in the extent of glycosylation of surface orientated proteins, with differences observed even between closely related species of primates. The failure to locate the large PAS-staining GP I band following SDS-polyacrylamide gel electrophoresis of cat platelet membranes, even though cat platelets have a comparable sialic acid content (21.3±2.3 ug per 109 platelets) to human platelets, may have implications concerning the proposed roles for this glycoprotein in platelet function. It is suggested that account should be taken of possible species differences in platelet surface structure during the interpretation of platelet function tests using animal models.
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