Interactions between insulins and liver membrane receptors of guinea pig, calf and chicken. Exclusion of a species-specific insulin receptor.

Insulin binding experiments were performed with liver plasma membranes from guinea pig, calf and chicken. Bound insulin was separated from free insulin by a simple and rapid centrifugation of membranes through a layer of silicon oil. 125 I-labeled beef insulin was displaced from receptor sites by unlabelled guinea pig, beef and chicken insulin. The receptors of animals with insulins of different biological activity show similar basic characteristics and affinities to the different insulin molecules and thus are not specialised for the interactions with the homologous insulin molecule. The binding capacity of the membranes for beef insulin seems to be inversely related to the affinity of the homologous insulin to the receptor, guinea pig membranes showing the highest and chicken membranes the lowest receptor concentration.