The cffect of chemical and enzymatic treatments on the biological activity of porcine follicle-stimulating hormone- releasing hormone (FSH-RH) was studied. FSH-RH activity was not affected by trypsin, pepsin, neuraminidase, carboxy- peptidasc A, aminopeptidase M and leucine aminopcptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidonc carboxylyl peptidase abolished the FSH-RI1 activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100°C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium mctaperiodate, and ninhydrin did not affect the FSH-RII activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Scr 1, Glu 1, Pro 1, Gly 2, Leu 1, Trp 1, and Tyr 1. These results and information obtained during purification procedures indicate that a basic polypeptide composed of ten amino acids possesses both LIl-RH and FSII-RH activity.
- FSH-relcasing hormone
- LH-releasing hormone
ASJC Scopus subject areas
- Endocrinology, Diabetes and Metabolism
- Endocrine and Autonomic Systems
- Cellular and Molecular Neuroscience