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Abstract
Luteinizing hormone receptor binding inhibitor (LH-RBI has been isolated from the aqueous extracts of ram testis using Sephadex column chromatography. Sephadex G-75 fraction I was found to inhibit the binding of I125 LH to rat testis receptors. Further purification of Sephadex G-75-I fraction on G-200 column gave four fractions (I-IV), the maximum inhibitory activity to inhibit I125 LH binding to rat testis receptor was associated with the fraction I only. Fraction II gave marginal inhibition only, whereas fractions III and IV did not have any inhibitory effect on I125 LH binding to rat testis receptors. Our findings suggest that LH-RBI isolated from ram testis is a protein having molecular weight more than 10,000 Daltons.
Published Version
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