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  • Title: Biological action and fate of photoaffinity-labelled insulin-receptor complexes.
    Author: Brandenburg D, Diaconescu C, Klotz G, Mucke P, Neffe J, Saunders D, Schüttler A.
    Journal: Biochimie; 1985; 67(10-11):1111-7. PubMed ID: 3907715.
    Abstract:
    Covalent linking of two photoactivatable insulin derivatives, B2-(2-nitro,4-azidophenylacetyl)-des-PheB1-insulin and B29-(2-nitro,4-azidophenylacetyl)-insulin to viable rat adipocytes gives a system, which contains a fixed stoichiometry between hormone and receptor. The biological signal of prolonged lipogenesis has been used to study several aspects of insulin binding and action: the role of the site of the crosslink between insulin and receptor, recognition of bound photoinsulin by anti-insulin antibodies, the half-life of the biologically active complex, the pH-dependence of the biological signal, and the possible role of internalization. Furthermore, the effect of trypsin on the insulin receptor, as well as the insulin-receptor complex, has been investigated and a refined model of the receptor is presented.
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