title: An improved method of purifying inhibin radioligand for radioimmunoassay.
abstract: Polyacrylamide gel electrophoresis (PAGE) separation of bovine inhibin from free iodine after iodination is described. Previous methods of separation typically relied upon a G25 gel filtration and Matrix gel Red A affinity column chromatography protocol. When compared to column chromatography, PAGE-purified radiolabelled inhibin resulted in significantly increased binding (13.1% vs. 7.5%) and enhanced sensitivity (ED50 = 92 microliters inhibin standard vs. ED50 = 198 microliters inhibin standard) to the inhibin antibody #1989. Our results demonstrate an advantageous approach to purifying 31,000 Mr bovine inhibin radioligand after iodination for RIA.
authors: Department of Medicine, Massachusetts General Hospital, Boston 02114.
authors: J R
authors: JR
authors: Bernstein
authors: W F
authors: WF
authors: Crowley
authors: A L
authors: AL
authors: Schneyer
mesh_terms: D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007265:Inhibins / Q000302:isolation & purification*; D008024:Ligands; D011863:Radioimmunoassay / Q000379:methods*
chemical_list: D008024:Ligands; D007265:Inhibins