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The proteolytic degradation of relaxin during its isolation from pregnant sow ovaries has been examined. Ovaries from pregnant sows were selected and divided into three groups according to the stages of pregnancy. Each group was extracted with and without protease inhibitors. It was found that protease(s) were present in all groups of ovaries and that a 2–4 fold increase in yield of total relaxin was obtained when isolation and purification was carried out in the presence of protease inhibitors. However the ratio of the three forms of relaxin remain unchanged.Relaxin is a small peptide hormone (M.W. 6,300) which relaxes the pubic symphysis, inhibits spontaneous uterine contractions, softens and dilates the cervix, and stimulates the development of mammary glands (1). Porcine relaxin has been successfully purified from pregnant sow ovaries (2). Three components, namely, CM-B, CM-a and CM-a' were obtained according to their order of elution from a CM-cellulose column. Although chemical structures for porcin...