Biol Reprod Keystone Symposia Conference on Frontiers in Reproductive Biology & Regulation of Fertility.
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Biology of Reproduction, Vol 29, 487-497, Copyright © 1983 by Society for the Study of Reproduction

ARTICLES

Two binding proteins for progesterone in the bovine corpus luteum

DL Willcox

The cytosolic supernatant of bovine corpus luteum contains two proteins which bind progesterone specifically. Bovine luteal cytosol was fractionated on hydroxylapatite and the peaks of protein obtained subjected to equilibrium dialysis against progesterone. Progesterone- binding activities (Ka approx. 10(6) 1/mol) was eluted at 40 mM (Binding Protein 1) and 100 mM phosphate (Binding Protein 2). They sedimented differently (3.95 and 4.65, respectively) on sucrose gradients. In contrast to Binding Protein 1, Binding Protein 2 bound R5020 better than progesterone on sucrose gradients. Purification of the binding activity eluted by 40 mM phosphate from the hydroxylapatite column showed that it resided in a single protein (molecular weight 65,000 daltons). The function of these proteins is presently unknown, but they may participate in the biosynthesis and/or secretion of progesterone from bovine luteal cells.




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Copyright © 1983 by the Society for the Study of Reproduction.