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A new technique for purification of the human sex hormone-binding globulin (SHBG) is described. This technique includes affinity chromatography of blood serum on cortisol-Sepharose, (NH4)2SO4 fractionation, gel filtration on a Bio-Gel P-300 column and chromatography on a concanavalin A-Sepharose 4B column. From 21 of retroplacental serum 10 mg of pure SHBG (25% yield) has been obtained. Upon gel filtration SHBG behaved as a biopolymer with Mr of 120,000. The molecular weight of SHBG as determined by electrophoresis was shown to be equal to 50,000. SHBG has a sedimentation constant of s20, w of 4.7S, pI of 5.75, extinction coefficient A1%(280,1cm) = 10,5 and association constants of 4.5 X 10(8) and 3.5 X 10(6) M-1 for 5 alpha-dihydrotestosterone and cortisol, respectively. The amino acid and carbohydrate contents of SHBG were determined.
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