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For the study of their various physiological and chemical properties, protein hormones in urine have usually been purified by adsorption or precipitation (Heller & Chandler, 1942; Bradbury, Brown & Brown, 1949; Johnsen, 1955; Albert, 1955; Butt, 1958; Loraine & Brown, 1959). Methods using kaolin adsorption followed by acetone precipitation have been widely used for the extraction of urinary gonadotrophins (HPG). However, for the immunochemical and biological characterization of isolated gonadotrophins, the kaolin-acetone method presents some potential drawbacks. Adsorption of the active constituents may be incomplete, and elution at the required high pH (11·5) as well as treatment with acetone may cause denaturation. Hobson & Wide (1964) have reported a decrease in the ratio of immunological properties to biological activity during the kaolin-acetone concentration of human chorionic gonadotrophin (HCG). In an attempt to minimize these difficulties, we have used ultrafiltration for the isolation of HPG. The results have been compared with