Presence of luteinizing hormone receptor binding inhibitor (LH-RBI) in ovine testis.
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.
D000818:Animals; D002850:Chromatography, Gel; D036341:Intercellular Signaling Peptides and Proteins; D007986:Luteinizing Hormone / Q000378:metabolism*; D008297:Male; D010455:Peptides; D011956:Receptors, Cell Surface / Q000037:antagonists & inhibitors* / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D011974:Receptors, LH; D012756:Sheep / Q000378:metabolism*; D013737:Testis / Q000032:analysis* / Q000378:metabolism
D036341:Intercellular Signaling Peptides and Proteins; C011898:LH receptor binding inhibitor; D010455:Peptides; D011956:Receptors, Cell Surface; D011974:Receptors, LH; D007986:Luteinizing Hormone