Abstract
We have recently purified a Mr 22,000 GTP-binding protein (G protein) to near homogeneity from human platelet membranes and characterized it (Ohmori, T., Kikuchi, A., Yamamoto, K., Kim, S. and Takai, Y. (1989) J. Biol. Chem. in press). This platelet G protein was present most abundantly among several G proteins in platelets and showed a Mr of about 22,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This platelet G protein showed kinetic and physical properties very similar to those of the novel smg-21 gene product, having the same putative effector domain as the ras gene products, which we have recently purified to near homogeneity from bovine brain membranes and characterized (Kawata, M., Matsui, Y., Kondo, J., Hishida, T., Teranishi, Y. and Takai, Y. (1988) J. Biol. Chem. in press). Moreover, the peptide map of the platelet G protein was identical with that of the smg-21 gene product and the partial amino acid sequence of the platelet G protein was identical with that of the smg-21 gene product. These results indicate that this human platelet G protein is the smg-21 gene product.