Insulin binding to liver plasma membranes from rats rendered diabetic by alloxan. A kinetic demonstration of two classes of binding sites in equilibrium with each other

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Abstract
The association of 125I-labeled insulin with liver plasma membranes from diabetic rats was consistent with more than 1 compartment of binding. After a short association period, insulin dissociation comprised rapid and slow phases. After a long association period, dissociation was only at a slow rate. Lower-affinity hormone-receptor complexes were converted to higher affinity complexes as the time of occupancy lengthened.