Abstract
Summary
A combination of exclusion chromatography on Bio-Gel P-10 and electrophoresis on a column of Sephadex G-25 at pH 9 has been used to isolate three proteins with relaxin activity from a porcine relaxin concentrate (NIH relaxin). The three proteins had similar molecular weights (∼5600) but different mobilities on polyacrylamide gels at pH 5.0 and 8.2. Two of them contained one residue of proline per mole. Bioassays indicated that one of the proline-containing relaxins was significantly less active in the guinea pig palpation assay than the other two, while retaining high activity in the rat uterine motility inhibition assay.
The authors are indebted to Dr. Wayne A. Chamley, of the Animal Research Institute, Werribee, Australia, for the rat uterine inhibition assays and to Elizabeth M. O'Byrne, of Ciba-Geigy Corp., Ardsley, New York for the immunochemical studies.
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