Particulate and solubilized LH receptor in the pig and bull testis.
Particulate and Triton X-100 solubilized receptors for luteinizing hormone (LH) in the pig and bull testis were studied. In some of the experiments tissue from the rat testis was included for comparison. LH receptors in the bull and pig revealed very similar association and dissociation kinetics, affinity (Kd = 1.2-1.8 x 10(-10) M), stability and physicochemical properties. Binding capacity was higher in the pig (73 fmol/mg protein) than in the rat (33 fmol/mg protein) and bull (17 fmol/mg protein). Hormone binding stabilized the receptor against thermal denaturation and temperature stability decreased upon solubilization. It is concluded that the properties of the testicular LH receptor of the pig and bull are very similar to those previously described from the rat.
D000818:Animals; D002417:Cattle / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D006358:Hot Temperature; D007700:Kinetics; D007986:Luteinizing Hormone / Q000378:metabolism; D008297:Male; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011974:Receptors, LH; D012995:Solubility; D013045:Species Specificity; D013552:Swine / Q000378:metabolism*; D013737:Testis / Q000378:metabolism*
D011956:Receptors, Cell Surface; D011974:Receptors, LH; D007986:Luteinizing Hormone