Santa-Coloma T A, Muschietti J P, Charreau E H
Comp Biochem Physiol A Comp Physiol. 1986;85(3):401-5. doi: 10.1016/0300-9629(86)90420-2.
The effects of temperature, pH, divalent cations, 2-mercaptoethanol (Et-SH), N-ethylmaleimide (NEM), and phenylmethylsulfonyl fluoride (PMSF) on the dihydrotestosterone (DHT) binding to sex steroid binding protein from Bufo arenarum (baSBP) were examined. The temperature curve indicated that the binding remained stable up to 50 degrees C and the pH curve showed maximum binding between pH 7 and 9. The incubations of baSBP with divalent cations, NEM and Et-SH demonstrated that baSBP require disulfides and sulfhydryl groups for steroid binding or to maintain an adequate protein conformation. On the other hand, PMSF had no effect on the binding, consequently, serine residues appear not to be involved in DHT binding to baSBP. These results indicate that baSBP has a behavior resembling that of human SBP.
研究了温度、pH值、二价阳离子、2-巯基乙醇（Et-SH）、N-乙基马来酰亚胺（NEM）和苯甲基磺酰氟（PMSF）对二氢睾酮（DHT）与沙蟾（Bufo arenarum）性类固醇结合蛋白（baSBP）结合的影响。温度曲线表明，在高达50摄氏度时结合保持稳定，pH曲线显示在pH 7至9之间结合最强。baSBP与二价阳离子、NEM和Et-SH的孵育表明，baSBP需要二硫键和巯基来结合类固醇或维持适当的蛋白质构象。另一方面，PMSF对结合没有影响，因此，丝氨酸残基似乎不参与DHT与baSBP的结合。这些结果表明，baSBP的行为类似于人类SBP。
