The proposed studies involve characterization of the physico-chemical nature of the insulin receptor in normal and insulin-resistant states. Attempts will be made to solubilize the insulin receptor from adipocyte and liver plasma membranes either in the presence or absence of insulin covalently cross-linked to the receptor. Polyacrylamide gel electrophoresis will be used to determine if the receptor has been altered during the development of the insulin resistant states. Other work is planned to further examine the mechanism by which the insulin-binding affinity of the receptor is markedly increased by the plant lectin, wheat germ agglutinin. These studies will employ the cross-linking reagent in studies with viable fat cells to determine if lateral mobility of the receptor or of other membrane constituents is required to obtain the increase in receptor affinity and insulin-sensitivity that accompanies treatment with the lectin.
