Key result
The synthetic analog des-Ser2-SCT was indistinguishable from salmon calcitonin in hypocalcemic activity and twice as potent for adenylate cyclase activation in renal membranes.
The deletion of the serine2 residue in salmon calcitonin does not impair its biological activity, indicating the intact ring structure function does not critically depend on its encompassed peptide chain length.
des-Ser2-SCT retains activity in animals; extends calcitonin structure-function data but leaves open human translation.
We studied the biological activity of a synthetic analog of salmon calcitonin (SCT), from which the serine2 residue within the amino-terminal disulfide ring had been omitted (des-Ser2-SCT). This analog proved to be indistinguishable from SCT with respect to hypocalcemic activity in vivo, displacement of [125I]SCT from rat renal membranes, and accumulation of cAMP in incubated renal cortical slices, des-Ser2SCT was twice as potent as SCT with respect to adenylate cyclase activation in renal membranes. Since the deletion did not impair biological activity, it appears that the function of the intact ring structure does not critically depend on its encompassed peptide chain length.
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Schwartz et al. (1981) studied this question. des-Ser2-SCT vs. salmon calcitonin (SCT) was evaluated on hypocalcemic activity in vivo, displacement of [125I]SCT, and accumulation of cAMP. The synthetic analog des-Ser2-SCT was indistinguishable from salmon calcitonin in hypocalcemic activity and twice as potent for adenylate cyclase activation in renal membranes.
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