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- W1566856537 abstract "Binding of 125I-labeled insulin and 125I-labeled NSILA-S (nonsuppressible insulin-like activity-soluble) to isolated perfused rat heart muscle was found to be a specific and saturable process. Saturation of binding was reached with both substances at concentrations which maximally stimulate glucose uptake in heart muscle. Whereas unlabeled NSILA-S displaced 125I-labeled insulin, the reverse did not occur. 125I-labeled insulin and 125I-labeled NSILA-S showed different dissociation kinetics. The half-lives of dissociation of insulin and NSILA-S were 17 and 26 min, respectively. It is suggested that the plasma membrane of rat heart muscle possesses two separate receptors, one for insulin and another one for NSILA-S. NSILA-S shows also some affinity for the insulin receptor." @default.
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- W1566856537 date "1976-11-01" @default.
- W1566856537 modified "2023-09-25" @default.
- W1566856537 title "Binding of insulin and nonsuppressible insulin-like activity to isolated perfused rat heart muscle" @default.
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- W1566856537 doi "https://doi.org/10.1016/0003-9861(76)90412-4" @default.
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