Use of fast protein liquid chromatography in the purification of inhibin from bovine follicular fluid.
Inhibin from bovine follicular fluid was partly purified using affinity chromatography on immobilized Procion Red 3B, gel filtration on Sephadex G-25 and ion-exchange chromatography on the fast protein liquid chromatography system. Inhibin was subsequently characterized using preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution. Biological activity was associated with a protein with an apparent molecular weight of approximately 65 kD.
D000818:Animals; D002417:Cattle; D002853:Chromatography, Liquid / Q000379:methods; D005122:Exudates and Transudates / Q000032:analysis*; D005260:Female; D007265:Inhibins / Q000302:isolation & purification*; D006080:Ovarian Follicle / Q000378:metabolism*
D007265:Inhibins