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Rabbit Testosterone-Binding Globulin. I. Physico-Chemical Properties

Centre de Recherches Endocrinologiques, Hopital Cochin, Paris France, and U 36 Research Unit, Paris, France

Abstract

Rabbit Testosterone—Binding—Globulin (R—TeBG) was demonstrated in rabbit plasma, and was distinct from Corticosteroid— Binding—Globulin and albumin. R—TeBG bound testosterone and its 17β—hydroxy and 5—reduced metabolites, 17β—estradiol and estrone. The affinity constant of R—TeBG for testosterone at 4 C was 6.16 X 10⁸M^-1 ± 1.45 (SD), the number of binding sites was 1.80 X 10^-7 ± 0.36 (SD) moles of testosterone per liter of normal, nonpregnant female plasma. Computed molecular radius (from Sephadex gel filtration and polyacrylamide gel electrophoresis) was 2.79, corresponding to a mol wt of 74000. Thus, the in vitro physical characteristics of R—TeBG are close to those of human TeBG. The rabbit should provide a useful model in which to study the effects of steroid protein binding on androgen metabolism. (Endocrinology 92: 1113, 197

Received July 20, 1972.