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Comparison between inhibin from human and bovine ovarian follicular fluid using fast protein liquid chromatography
Inhibin from human and bovine ovarian follicular fluid was purified 700-900-fold using affinity chromatography on immobilized Procion Red 3B, desalting on Sephadex G-25, ion-exchange chromatography on the fast protein liquid chromatography (FPLC) columns Mono Q and Mono P and chromatography on immobilized lectins. Isoelectric points for inhibin from human and bovine origin were between 5.1-5.7 and 4.75-5.25, respectively. Inhibin from both sources was retained by immobilized lectins, indicating its association with a glycoprotein. Overall recoveries of inhibin activity after these chromatographic procedures were approximately 1%.
Inhibin from human and bovine ovarian follicular fluid was purified 700-900-fold using affinity chromatography on immobilized Procion Red 3B, desalting on Sephadex G-25, ion-exchange chromatography on the fast protein liquid chromatography (FPLC) columns Mono Q and Mono P and chromatography on immobilized lectins. Isoelectric points for inhibin from human and bovine origin were between 5.1-5.7 and 4.75-5.25, respectively. Inhibin from both sources was retained by immobilized lectins, indicating its association with a glycoprotein. Overall recoveries of inhibin activity after these chromatographic procedures were approximately 1%.