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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-06-16
    Description: Antibodies to insulin receptors purified from rat liver membranes do not complete with [125I]insulin for binding to the insulin receptor but do precipitate solubilized receptors labeled with [125I]insulin. These antibodies have the insulin-like activities of enhancing glucose oxidation and inhibiting epinephrine-induced lipolysis in rat adipocytes. Thus, antibody binds to the receptor at a different site from that to which insulin binds, yet the interaction can initiate an effective biological response. These results indicate that the previously studied insulin-binding sites are the physiological macromolecular receptors for insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, S -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1283-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663609" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthosis Nigricans/physiopathology ; Adipose Tissue/metabolism ; Animals ; *Antibodies ; Antigen-Antibody Reactions ; Binding Sites ; Binding, Competitive ; Biological Transport ; Epinephrine/pharmacology ; Glucose/metabolism ; Insulin/metabolism ; Lipid Mobilization ; Liver/immunology ; Rats ; Receptor, Insulin/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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