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. 1965 Jan;94(1):150–159. doi: 10.1042/bj0940150

Antagonism of insulin action on muscle by the albumin-bound B chain of insulin

J W Ensinck 1,*, R J Mahler 1, J Vallance-Owen 1
PMCID: PMC1206421  PMID: 14342222

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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