Abstract
A significant further purification of postmenopausal urinary luteinizing hormone [LH] has been obtained by a combination of carboxymethyl-cellulose chromatography and Sephadex G-100 gel filtration. A feature of the latter procedure was the use of highly purified human pituitary luteinizing hormone to calibrate the G-100 column, thus defining the area of the elution profile where the purified urinary luteinizing hormone would be expected to emerge. The specific activity of the final lyophilized product was 0.081 NIH-LH-Sl U/mg (OAAD assay) and the FSH/LH ratio was less than 3.1. In terms of the 2nd IRP-HMG [human menopausal gonadotropin], the specific activity was 124.8 IU/mg, and the FSH [follicle-stimulating hormone]/LH ratio was less than 0.052. The purified urinary LH fraction was not homogeneous when examined by polyacrylamide gel electrophoresis.