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ANTAGONISM OF INSULIN ACTION ON MUSCLE BY THE ALBUMIN-BOUND B CHAIN OF INSULIN

1965; Portland Press; Volume: 94; Issue: 1 Linguagem: Inglês

10.1042/bj0940150

0006-2936

J. Ensinck, RJ Mahler, J. Vallance‐Owen,

Mitochondrial Function and Pathology

1. The presence of a substance associated with human albumin that exerts anti-insulin activity on the isolated rat diaphragm has been confirmed. This factor has been removed from albumin, thereby providing a source of non-antagonistic carrier protein. 2. Derivatives of the polypeptide B chain of insulin obtained by chemical scission of the interchain disulphide bonds have been separated by conventional techniques. In the presence of non-antagonistic albumin, the reduced and sulpho-B chain preparations inhibited insulin action on muscle. 3. The B chain resulting from reductive cleavage of insulin by bovine-liver extracts, in association with human albumin, exhibited a comparable anti-insulin effect. 4. It is postulated that the B chain interacts with albumin to enable solubilization of the chain and that inhibition of insulin action on muscle may occur as a result of competition for cellular receptor sites by the B chain. 5. The implication of these findings in relation to a circulating insulin antagonist is discussed.