The use of affinity matrices in the purification of inhibin from bovine follicular fluid

Abstract

The protein associated with inhibin-like activity in bovine follicular fluid was purified 80- to 120-fold after successive adsorptions on different affinity matrices, i.e. Matrex gel red A, phenyl sepharose, omega-aminohexyl agarose and concanavalin-A sepharose. Partial characterization of the active protein resulted in the conclusion that inhibin from bovine follicular fluid is a hydrophobic glycoprotein with an apparent molecular weight between 60 000 and 70 000 daltons. An antiserum, raised against an 80-fold purified preparation, prevented the inhibin-like action of bovine follicular fluid on pituitary cells in vitro.