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Primary structure of porcine relaxin: homology with insulin and related growth factors

Nature volume 267, pages 544–546 (1977)Cite this article

Abstract

HISAW and co-workers1,2 first described a factor from sow corpora lutea that caused relaxation of the pubic symphysis in oestrogen-primed guinea pigs. Subsequent studies have shown that the active substance, termed relaxin, is a low molecular weight peptide hormone. Its presence has been demonstrated during pregnancy in female pigs, guinea pigs, rabbits, mice and rats3,4, and, more recently, in humans5. Its actions include dilatation and softening of the cervix, inhibition of uterine contractions and relaxation of the pubic symphysis and other pelvic joints. Relaxin, which has a molecular weight of approximately 6,000, consists of two non-identical chains joined by disulphide bridges6. We have now determined, and report here, the complete amino acid sequence of porcine relaxin.

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Authors and Affiliations

  1. Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria, Australia, 3052

    ROBERT JAMES & HUGH NIALL

  2. Department of Anatomy and Reproductive Biology, University of Hawaii, Honolulu, USA

    SIMON KWOK & GILLIAN BRYANT-GREENWOOD

Authors
  1. ROBERT JAMES
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  2. HUGH NIALL
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  3. SIMON KWOK
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  4. GILLIAN BRYANT-GREENWOOD
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JAMES, R., NIALL, H., KWOK, S. et al. Primary structure of porcine relaxin: homology with insulin and related growth factors. Nature 267, 544–546 (1977). https://doi.org/10.1038/267544a0

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