Abstract
The 34-amino acid NH 2-terminal fragment of human parathyroid hormone synthesized according to the sequence described by Niall et al. (1) is approximately 140 times more potent than the fragment synthesized according to Brewer et al (2) in activating human renal cortex adenylate cyclase. The potencies of the two peptides, relative to the effect of MRC standard bovine parathyroid hormone preparation 67 342 in this system, were 5600 ± 600 (S.E.M.) units/mg and 40 ± 5 units/mg respectively. The potencies of the more active peptide and the corresponding bovine parathyroid hormone sequence were similar in this system and also in assays based upon the production of cyclic AMP by chick kidney both in vivo and in vitro .
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