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• W2116739144 abstract "High affinity binding sites have been found in membrane preparations from hamster β-cell tumors by using radiolabeled gastric inhibitory polypeptide (125I-GIP). HPLC of 125I-GIP resulted in two major peaks (A III and B III), with identical specific binding. It was verified that peaks A III and B HI stimulate insulin release from the isolated perfused rat pancreas to an extent at least equal to that obtained with unlabeled GIP at 10−9m. Natural GIP competitively inhibited the binding of 125I-GIP in the range of 10−10–10−6m and half-maximal inhibition was observed at 1.9 ± 0.19 x 10−9m GIP. The number of high affinity sites was 219 ± 8 fmol/mg protein and the dissociation constant was 2.05 ± 0.1 × 10−9m. None of 10 regulatory peptides tested exhibited any effect on the 125I-GIP binding at concentrations in the range of 10−6–10−4m. Consequently, saturable, high affinity and specific binding sites for the GIP have been found and characterized in the plasma membranes of β-cells. This model can be of use in studying the interaction of GIP with its preponderant target tissue. (Endocrinology115: 1324–1331, 1984)" @default.
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• W2116739144 date "1984-10-01" @default.
• W2116739144 modified "2023-10-01" @default.
• W2116739144 title "Evidence for and Characterization of Specific High Affinity Binding Sites for the Gastric Inhibitory Polypeptide in Pancreatic<i>β</i>-Cells*" @default.
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• W2116739144 doi "https://doi.org/10.1210/endo-115-4-1324" @default.
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