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Abstract
The effect 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, carboxypeptidase A, aminopeptidase M and leucine aminopeptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidone carboxylyl peptidase abolished the FSH-RH activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100 °C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium metaperiodate, and ninhydrin did not affect the FSH-RH activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Ser 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 LH-RH and FSH-RH activity.
Published Version
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