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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 May;81(9):2640–2644. doi: 10.1073/pnas.81.9.2640

Amino acid sequence of homologous rat atrial peptides: natriuretic activity of native and synthetic forms.

N G Seidah, C Lazure, M Chrétien, G Thibault, R Garcia, M Cantin, J Genest, R F Nutt, S F Brady, T A Lyle, et al.
PMCID: PMC345125  PMID: 6232612

Abstract

A substance called atrial natriuretic factor (ANF), localized in secretory granules of atrial cardiocytes, was isolated as four homologous natriuretic peptides from homogenates of rat atria. The complete sequence of the longest form showed that it is composed of 33 amino acids. The three other shorter forms (2-33, 3-33, and 8-33) represent amino-terminally truncated versions of the 33 amino acid parent molecule as shown by analysis of sequence, amino acid composition, or both. The proposed primary structure agrees entirely with the amino acid composition and reveals no significant sequence homology with any known protein or segment of protein. The short form ANF-(8-33) was synthesized by a multi-fragment condensation approach and the synthetic product was shown to exhibit specific activity comparable to that of the natural ANF-(3-33).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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