Purification of Follicle-Stimulating Hormone-Releasing Factor (FSH-RF) from Bovine Hypothalamus

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Abstract
Acetic acid extracts of bovine hypothalamic tissue were concentrated by a precipitation procedure and subjected to gel filtration on Sephadex. Follicle-stimulating hormone-releasing factor (FSH-RF) activity was followed by measuring depletion of follicle-stimulating hormone (FSH) from pitultaries of normal, or castrated testosterone-treated male rats, as well as elevation of plasma FSH activity in castrated female rats treated with estrogen and progesterone. FSH-RF activity was found consistently to emerge from Sephadex just after [beta]-MSH and before luteinizing hormone-releasing factor (LRF) and vasopressin. Bovine FSH-RF purified by gel filtration on Sephadex is essentially free of LRF. The LRF active fractions from Sephadex do not show any FSH-RF activity. The FSH-RF zone from Sephadex was further purified by phenol extraction and then chromatographed on carboxymethylcellulose (CMC). This step separated FSH-RF from thyrotropic hormone-releasing factor (TRF). Purified FSH-RF was active in vivo at the level of 10-47 [mu]g, Chemical and biological characteristics indicate that FSH-RF is different from oxytocin, vasopressin, [alpha]- and [beta]-MSH, LRF and TRF.