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An improved method of purifying inhibin radioligand for radioimmunoassay
J R Bernstein1, W F Crowley, A L Schneyer
1Department of Medicine, Massachusetts General Hospital, Boston 02114.
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.
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.