Yue D K, Baxter R C, Turtle J R
Biochim Biophys Acta. 1976 Aug 24;444(1):231-9. doi: 10.1016/0304-4165(76)90240-3.
The dissociation of insulin from human insulin antibodies has been investigated using a technique that is rapid and does not require addition of excess unlabelled insulin. A slow (k1 = 2-10(-3) min-1) and a fast k2 = 4-10(-2) min-1) dissociating antibody component were identified in all studies. These have been shown to correspond, respectively, to the high and low affinity antibody components of equilibrium binding studies. The range of k1 and k2 values and their response to temperature change is small. Insulin resistance and stability of diabetes are not related to properties of antibody dissociation. Dissociation is faster in the presence of high (6-850 nM) insulin concentration due to increased binding to the fast dissociating component without change in the dissociation rate constants. When incubation time is increased beyond achievement of maximal binding there is a time-depent rise in binding to the slow dissociating component, with a concomitant fall in k1. The traditional concept that equilibrium is established at maximum binding requires further examination.
