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The concept of nonsteroidal regulators of gonadotrophin secretion originated with the identification of inhibin \p=n-\a hormone produced by the gonads that selectively inhibits the secretion of pituitary follicle stimulating hormone (FSH) \p=n-\the existence of which was postulated some 70 years ago (Mottram and Cramer, 1923; McCullagh, 1932). However, the purification and characterization of inhibin was a long and arduous task confounded by many factors, including the wide range of starting materials, the different bioassay systems used to define and estimate inhibin activity, the properties of the protein that rendered it resistant to standard protein purification techniques, and the absence of a generally accepted reference preparation for inhibin activity (Findlay, 1986). In addition to being a member of a wider family of proteins with diverse biological activities in a number of systems, inhibin itself is a complex protein existing as different molecular mass forms as well as products of different genes (for example see Findlay, 1986; Mason et al, 1986; Stewart et al, 1986; Robertson et al, 1992). Inhibin is now known to be a heterodimeric glycoprotein composed of an subunit and a ß subunit which are not covalently linked. The ß subunit occurs in two different forms, termed ß and ß , giving rise to inhibin A and inhibin on combination with the subunit. The ß subunits are also known to combine together to give rise to a molecule which is termed activin on account of its ability to stimulate FSH secretion from the pituitary. Activin can exist in at least three forms: activin A, activin AB and activin B, depending upon the ß subunit composition. Robertson et al. (1995, 1996), using a fractionation procedure, reported the identification of a range of bioactive and immunoactive forms of inhibin in human plasma. These forms have molecular

Commentary: standardization of nonsteroidal regulators of gonadotrophin secretion