Abstract

1. The luteinizing hormone activity in gonadotropin preparations from human and equine pituitaries, human chorionic gonadotropin and pregnant mare serum was inactivated by digestion with alpha-chymotrypsin. By contrast, the luteinizing hormone activity of a human postmenopausal urinary gonadotropin preparation was resistant to enzymic digestion. 2. As with human, ovine and porcine pituitary gonadotropin preparations, human postmenopausal urinary follicle stimulating hormone was not inactivatedinactivated by chymotryptic digestion. This hormonal activity, however, was destroyed by the enzyme in preparations from equine pituitaries and pregnant mare serum. 3. The results suggest that differences exist between pituitary and urinary LH, and between equine FSH and FSH from the other sources studied. These dissimilarities are presumably a reflection of structural differences in the neighborhood of the biologically active site on these hormones. (Endocrinology 84: 9, 1969)

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