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. 1974 Feb;71(2):384–388. doi: 10.1073/pnas.71.2.384

The Amino-Acid Sequence of the Amino-Terminal 37 Residues of Human Parathyroid Hormone

H D Niall *, R T Sauer *, J W Jacobs *, H T Keutmann *, G V Segre *, J L H O'Riordan †, G D Aurbach ‡, J T Potts Jr *
PMCID: PMC388010  PMID: 4521809

Abstract

The sequence of the amino-terminal 37 residues of human parathyroid hormone has been established. The hormone used in these studies was isolated in highly purified form from parathyroid adenomata and was subjected to automated degradation in a Beckman sequencer. A high-sensitivity sequencing procedure employing 35S-labeled phenylisothiocyanate of high specific activity as the coupling agent was used. The sequence obtained differs from that of bovine parathyroid hormone in three of the first 37 positions, and from that of porcine parathyroid hormone in two positions. A single human-specific residue was found (asparagine 16). The sequence obtained differs at three positions (22, 28, and 30) from the structure for human parathyroid hormone reported recently by Brewer et al. [(1972) Proc. Nat. Acad. Sci. USA 69, 3585-3588] and synthesized by Andreatta et al. [(1973) Helv. Chim. Acta, 56, 470-473] We have carefully reviewed our data, reported here in detail, on the sequence positions in dispute. We must conclude, on the basis of all available data, that the structure that we propose is the correct structure. The objective resolution of these discrepancies in structural analysis through further chemical and immunochemical studies is important, since synthesis of human parathyroid hormone, in which there is widespread interest for physiological and clinical studies, must be based on the correct sequence of the human hormone if the peptide is to be genuinely useful.

Keywords: high-sensitivity automated Edman degradation, radio-iodination, peptide synthesis, immunoreactivity

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Selected References

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