Abstract
Synthetic secretin has been iodinated at the N-terminal histidine, leading to an almost 100% yield of mono- and diiodo-secretin (“lodo-secretin”). The catalytic exchange of iodine against tritium results in the preparation of secretin labeled with tritium mainly at the histidine residue (7 Ci/mmol). Iodo-secretin and [ 3H]secretin have the same potency in stimulating pancreatic adenylate cyclase as secretin, but the apparent affinity of [ 3H]secretin for this enzyme is twice as high as for iodo-secretin. [ 3H]Secretin binds rapidly to pancreatic plasma membranes. Adding excess unlabeled secretin reduces the tracer binding by about 70%.
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