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Proteins of the turkey erythrocyte membrane.

A new and simplified method is described for preparation of turkey erythrocyte membranes which are essentially devoid of supernatant or nuclear contamination, but retain catecholamine-sensitive adenylate cyclase activity. These membranes have been solubilized in sodium dodecyl sulfate and analyzed by polyacrylamide gel electrophoresis and the major protein components identified. The turkey erythrocyte membranes exhibit a protein profile very similar to that of the human erythrocyte membrane, but contain a protein component of apparent molecular weight of 50000 which is not present in the human membranes. Three surface glycoprotein components of the turkey erythrocyte membranes (apparent molecular weights of 90000, 41000, and 26000) have been identified by periodic acid-Schiff staining of polyacrylamide gels and by cell surface 125I labeling using lactoperoxidase followed by polyacrylamide gel electrophoresis. After deoxycholate solubilization of membranes prepared from iodinated cells, glycoprotein with molecular weights of 90000 and 41000 bind to an infinity column of concanavalin A-Sepharose 4B and elute upon application of methyl alpha-Dmannopyrannoside. The lowest molecular weight glycoprotein component, however does not bind to the insolubilized concanavalin A.