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.
The association of 125I-labelled insulin with liver plasma membranes from diabetic rats was consistent with more than one 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.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002850:Chromatography, Gel; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism*; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D007457:Iodine Radioisotopes; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000378:metabolism*; D013997:Time Factors
D007328:Insulin; D007457:Iodine Radioisotopes; D011972:Receptor, Insulin