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• W324069378 abstract "ABSTRACT Recent results of the protein and subunit structure of the insulin receptor are described. The use of purified receptor, and the techniques of affinity labeling and crosslinking has been particularly valuable. The native receptor appears to be a heterotetramer of MW of about 300,000, consisting of two subunits of 130,000 and two subunits of 90,000 MW which are disulfide linked and in addition are held together by strong non-covalent forces. The 90,000 component is readily nicked by proteolysis to yield a 45,000 component (still capable of binding insulin). Antibodies raised against the purified receptor or the 130,000 MW subunit do not block insulin binding but are capable of eliciting the immediate metabolic effects of insulin in various tissues. An unusual clinical syndrome characterized by insulin-resistant diabetes mellitus and acanthosis nigricans is associated with circulating anti-receptor antibodies which inhibit insulin binding and which mimic insulin's biological responses in vitro. The latter effects are dependent on bivalent receptor crosslinking by the antibody. The role of receptor aggregation in mediating insulin responses is considered to be of possible biological significance." @default.
• W324069378 created "2016-06-24" @default.
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• W324069378 date "1982-01-01" @default.
• W324069378 modified "2023-09-27" @default.
• W324069378 title "Insulin Receptor Structure and Antibodies" @default.
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• W324069378 doi "https://doi.org/10.1016/b978-0-08-028022-6.50024-2" @default.
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