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Journal of Clinical Endocrinology & Metabolism, Vol 52, 601-604, Copyright © 1981 by Endocrine Society


ARTICLES

Relaxin purification from human placental basal plates

S Yamamoto, SC Kwok, FC Greenwood and GD Bryant-Greenwood

A crude relaxin preparation has been obtained from the basal plate region of electric cesarean section human placentae, as well as normal term placentae. The relaxin isolated has different charge properties by ion exchange chromatography from porcine relaxin, although it is of approximately the same molecular size. The most potent fraction obtained has approximately 0.7% of the immunoactivity of purified porcine relaxin when compared with porcine relaxin in a RIA based on porcine material, suggesting significant amino acid sequence differences between the putative human relaxin and its porcine counterpart.


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E. Masini, S. Nistri, A. Vannacci, T. B. Sacchi, A. Novelli, and D. Bani
Relaxin Inhibits the Activation of Human Neutrophils: Involvement of the Nitric Oxide Pathway
Endocrinology, March 1, 2004; 145(3): 1106 - 1112.
[Abstract] [Full Text] [PDF]




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