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The interaction of insulin and insulin receptor was studied with rat liver plasma membranes. Rat liver was homogenized with a Polytron PT 20 ST and fractionated by differential centrifugation. Prepared plasma membranes (100 gag protein) were incubated with enzymatically iodinated '"I-insulin (0.3 ng, specific activity 107 suCi/pg) in 25 mM Tris-HC1 buffer, pH 7.5, containing 0.9% NaC1 and 1% bovineserum albumin. The membranes which bound with insulin were separated from freeinsulin by filtration on millipore filters (EGWP) and the filters were washed with 5ml of the ice-cold buffer. Radioactivity on the filters was counted in an autogamma spectrometer. The results obtained were as follows: 1) The 12,000xgand 17,000xg-sediments obtained after subfractionation of liver homogenates showed almost equally high specific binding activity with 125I-insulin and less activity was detected in the 600 g,5,000 gand 40,000 gsediments and the 40,000 gsupernatant. 2) Specific binding of insulin with the membrane fraction was time-, temperatureand ionic strength-dependent. The highest binding was obtained under conditions in which the membrane fraction was incubated with insulin for 24 hours at 4°C in the buffer containing 1 M NaCl. Under these conditions, specific binding of '"I-insulin was 26.8% of the total radioactivity.

Studies on Interaction of Insulin and Insulin Receptor in Rat Liver Cell Membranes