PMID: 6987119Apr 1, 1980Paper

Hagfish insulin: the discrepancy between binding affinity and biologic activity

Diabetes
S O EmdinJ Gliemann

Abstract

Hagfish insulin exhibits a binding affinity of about 25% of that of pig insulin in rat adipocytes and IM-9 lymphocytes, even though its relative biologic potency is only about 5% in adipocytes. The dissociation rate constant of hagfish insulin is about half that of pig insulin, and the association rate constant is about one eighth. A longer time is, therefore, required for hagfish insulin to reach a steady state of binding. Failure to reach steady state is the probable reason why some previous results suggested a relative binding affinity of hagfish insulin of the same magnitude as the relative biologic potency.

Citations

May 1, 1994·European Journal of Biochemistry·L Schäffer
Apr 1, 2005·The Journal of Biological Chemistry·Jonathan Whittaker, Linda Whittaker

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