链霉素和蛋白质结合对蛋白质构象的影响

CHANGES OF PROTEIN CONFORIVIATION BY STREPTOMYCIN INTERACTING WITH PROTEIN

利用波谱分析(DSC、紫外光谱、荧光光谱)的方法,证明SM和BSA的共价结合或非共价结合,都可使得BSA的构象发生改变。BSA中一些芳香族氨基酸由内部疏水区外露,使得BSA的紫外光谱蓝移、荧光光谱红移。SM对BSA构象的影响较双氢链霉素(DHS)强。根据实验结果,对SM分子在体内产生SM抗体的机制进行了讨论。

Evident changes of the protein conformation could be found by spectrum analyses(DSC, UV and FLUOR), while streptomycin(SM)interacted with bovine serum albumin(BSA). Some aryl-amino acids of the BSA were exposed from the inner hydrophbic region,which caused the hypsochromic shift of UV spectrum and the bathochromic shift of fluorecence spectrum. The effects of dihydrostreptomycin(DHS) was weaker than of SM. The mechanism of SM inducing body to form the antibody was also discussed.