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  • Title: Receptor-binding kinetics of A-14 and A-19 125I-labelled insulin.
    Author: Watanabe N, Kobayashi M, Ohgaku S, Iwasaki M, Maegawa H, Shigeta Y.
    Journal: Biochim Biophys Acta; 1984 Apr 24; 798(3):313-6. PubMed ID: 6370314.
    Abstract:
    Receptor-binding kinetics and degradation of tyrosine A-14 and A-19 125I-labelled insulin was studied using cultured human lymphocytes. Receptor-binding ability of A-14 insulin was 1.5-times as high as that of A-19 insulin. Dissociation from receptors on lymphocytes showed no difference between these two labelled insulins. In association studies percent bound of A-14 insulin was 1.5-times as high as that of A-19 insulin at any time after incubation. These results suggested that lower binding affinity of A-19 insulin was due to decreased association rate, but not due to increased dissociation rate. Degradation of A-14 insulin by incubation media of lymphocytes was also 1.5-times as high as that of A-19 insulin.
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