title: Use of fast protein liquid chromatography in the purification of inhibin from bovine follicular fluid.
abstract: 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.
mesh_terms: 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*
chemical_list: D007265:Inhibins