Abstract
The striking structural homology with insulin suggests that relaxin may also be derived from a 9,000 dalton single peptide chain precursor. Therefore, in the past few years, we have been searching for a precursor of relaxin using two different approaches, namely, a) isolation of the precursor from pregnant sow ovaries and b) demonstration of the precursor in in vitro biosynthetic studies.
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Kwok, S. C. M., Bryant-Greenwood, G. D. and Niall, H. D. (1980). Evidence for proteolysis during purification of relaxin from pregnant sow ovaries. Endocr. Res. Commun. 7:1.
Kwok, S. C. M., Chamley, W. A. and Bryant-Greenwood, G. D. (1978). High molecular weight forms of relaxin in pregnant sow ovaries. Biochem. Biophys. Res. Commun. 82:997.
Sherwood, O. D. and O’Byrne, E. M. (1974). Purification and characterization of porcine relaxin. Arch. Biochem. Biophys.
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© 1982 Plenum Press, New York
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Kwok, S.C.M., Yamamoto, S.Y. (1982). Isolation and Characterization of High Molecular Weight Forms 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_17
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DOI: https://doi.org/10.1007/978-1-4613-3368-5_17
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