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- W1565859051 abstract "Abstract Glucagon-sensitive, insulin-secreting tumors of the Syrian (golden) hamster were homogenized in 1 mm NaHCO3 and subjected to differential centrifugation. The 10,000 x g particles were used for both binding of 125I-glucagon and activation of adenylate cyclase. Glucagon was the only hormone that activated adenylate cyclase. 125I-Glucagon bound to receptors rapidly and was competitively displaced by 1 µg per ml or less of unlabeled hormone; other polypeptide hormone were without effect. The glucagon concentration that produced half-maximal activation of adenylate cyclase was 10 ng per ml and half-maximal displacement of 125I-glucagon was 5 ng per ml; 2–29 glucagon, missing only the NH2-terminal histidine, bound to receptors but did not activate adenylate cyclase. When 2–29 glucagon was added to native glucagon, it blocked activation of adenylate cyclase. Extracts of porcine that contained glucagon immunoreactivity also activated adenylate cyclase but were only one-tenth as potent as pancreatic glucagon; 2–29 glucagon inhibited the effect of gut glucagon." @default.
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- W1565859051 date "1972-02-01" @default.
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- W1565859051 title "Glucagon Receptors in β-Cells" @default.
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- W1565859051 doi "https://doi.org/10.1016/s0021-9258(19)45636-6" @default.
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