Abstract
The endocrinological events leading to parturition are poorly understood. There are obvious species differences and no generalizations are possible at this time. In 1926 Hisaw called attention to the fact that in some mammals an ovarian factor is produced that leads to an enlargement of the birth canal in preparation for parturition. Subsequent work showed that this factor suppressed uterine contractions that might be harmful to the fetus. Hisaw and his coworkers also demonstrated that this ovarian factor was not a steroid but a protein susceptible to proteolytic action. He determined some physical properties of his new factor, relaxin, and compared them in an almost visionary fashion with the properties of insulin. Importantly, the involvement in parturition of a distinct hormone was demonstrated for the first time. The next thirty years of relaxin research was dominated by studies concerning the physiology of relaxin. The investigation of the biochemistry of relaxin suffered from the absence of an accurate and convenient bioassay. In 1930 Fevold et al. introduced the guinea pig assay which was rather elaborate and not sufficiently objective. The introduction of the mouse assay system by Steinetz et al. (1959) and the discovery of Kliman and Greep (1958) that the activity of relaxin in mice could be enhanced more than 100-fold by simultaneous injection of an adjuvant provided a better basis for the purification of relaxin.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Bedarkar, S., Turnell, W. G., Blundell, T. L. and Schwabe, C. (1977). Relaxin has conformational homology with insulin. Nature 270: 449.
Cohen, H., (1963). Relaxin: studies dealing with isolation, purification, and characterization. Trans. N.Y. Acad. Sci. 25: 313.
Doczi, J. (1963). Process for extraction and purification of relaxin. U. S. Patent 3,096,246.
Fevold, H., Hisaw, F. L., and Meyer, R. K. (1930). The relaxative hormone of the corpus lutuem. Its purification and concentration. J. Am. Chem. Soc. 53: 3340.
Frieden, E. H. (1963). Purification and electrophoretic properties of relaxin preparations. Trans. N. Y. Acad. Sci. 25:331.
Griss, G., Keck, J., Engelhorn, R. and Tuppy, H. (1967). The isolation and purification of an ovarian polypeptide with uterine relaxin activity. Biochim. Biophys. Acta 140: 45.
Hisaw, F. L. (1926). Experimental relaxation of the pubic ligament of the guinea pig. Proc. Soc. Exp. Biol. Med. 23:661.
James, R., Niall, H., Kwok, S. and Bryant-Greenwood, G. (1977). Primary structure of porcine relaxin: homology with insulin and related growth factors. Nature 267: 544.
Kliman, B. and Greep, R. 0. (1958). The enhancement of relaxin-induced growth of the pubic ligament in mice. Endocrinology 63: 586.
Schwabe, C. and Braddon, S. (1976). Evidence for one essential tryptophan residue at the active site of relaxin. Biochem. Biophys. Res. Commun. 68: 1126.
Schwabe, C. and McDonald, J. K. (1977). Relaxin: a disulfide homolog of insulin. Science 197: 914.
Schwabe, C., McDonald, J. K. and Steinetz, B. (1976). Primary structure of the A chain of porcine relaxin. Biochem. Biophys. Res. Commun. 70: 397.
Schwabe, C., McDonald, J. K. and Steinetz, B. (1977). Primary structure of the B chain of porcine relaxin. Biochem. Biophys. Res. Commun. 75: 503.
Sherwood, O. D. and O’Byrne, E. M. (1974). Purification and characterization of porcine relaxin. Arch. Biochem. Biophys. 160: 185.
Sherwood, O. D. (1979). Purification and characterization of rat relaxin. Endocrinology 104: 886.
Steinetz, B., Beach, V. L. and Kroc, R. L. (1959). The physiology of relaxin in laboratory animals, in: “Recent Progress in the Endocrinology of Reproduction”, C.H. Lloyd, ed., Academic Press New York.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1982 Plenum Press, New York
About this chapter
Cite this chapter
Schwabe, C., McDonald, J.K., Steinetz, B.G. (1982). On the Structure and Function of Relaxin. In: Anderson, R.R. (eds) Relaxin. Advances in Experimental Medicine and Biology, vol 143. Springer, New York, NY. https://doi.org/10.1007/978-1-4613-3368-5_7
Download citation
DOI: https://doi.org/10.1007/978-1-4613-3368-5_7
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4613-3370-8
Online ISBN: 978-1-4613-3368-5
eBook Packages: Springer Book Archive