Partial Purification and Separation of Human Pituitary Gonadotrophins1

Abstract

A major separation and a high purification of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH, ICSH) activities of human pituitaries, in good yield, were achieved by column chromatography on DEAE-cellulose. The principal FSH-containing fraction was 29 times more potent than NIH-FSH-S1, according to the HCG-augmentation assay of Steelman and Pohley. In terms of other reference preparations, the FSH activity of this fraction was 53 times greater than the Armour Standard FSH, and 5820 times greater than HMG-24. According to the ovarian ascorbic acid depletion assay of Parlow, the principal LH-containing fraction was 0.9 times as potent as NIH-LH-S1, and 2768 times more potent than HMG-24. Also, it is equivalent to 500 IU of International Standard HCG per mg. Furthermore, the contamination of this LH preparation with FSH was low, 0.1 times NIH-FSH-S1 per mg. The lyophilized preparation of human FSH is more potent than any previously isolated. The ratio of FSH:LH activity in the principal FSH fraction was 4820 times higher than this ratio in the principal LH fraction. (Endocrinology74:, 236, 1964)