A thermodynamic approach to hormone-receptor interaction; application to insulin binding to adipocytes, adipocyte plasma membranes and liposomes incorporating adipocyte insulin receptors.
The binding of insulin to its receptor in rat adipocyte and isolated plasma membranes has been measured. The adipocyte insulin receptor has been reconstituted in lecithin liposomes and the binding of insulin investigated. A method of interpreting binding data presented as binding vs. the logarithm of free insulin concentration (binding isotherms) in terms of the binding potential concept of Wyman (1965) is described, and the results are compared with the commonly used Scatchard analysis of binding. The binding potential approach enables binding constants and Gibbs energies of formation of the insulin-receptor complex to be determined as a function of insulin bound. The limiting Gibbs energies of binding at 15 degrees C to intact cells, membranes and liposomes were found to be -55, -52 and -49 kJ mol-1 respectively. The affinity of the receptor for insulin decreases smoothly with increase in binding in all three systems. For intact adipocytes the number of insulin receptors per cell is found to be approximately 43,000.
Jones
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Riley
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D000273:Adipose Tissue / Q000166:cytology / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D007700:Kinetics; D008081:Liposomes / Q000378:metabolism*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000378:metabolism*; D013010:Sonication; D013816:Thermodynamics
D007328:Insulin; D008081:Liposomes; D011972:Receptor, Insulin