Jacobson S C, Andersson S, Allenmark S G, Guiochon G
Department of Chemistry, University of Tennessee, Knoxville.
Chirality. 1993;5(7):513-5. doi: 10.1002/chir.530050707.
On a column with bovine serum albumin (BSA) immobilized covalently to silica, the adsorption isotherms of the enantiomers of mandelic acid, tryptophan, 2-phenylbutyric acid, and N-benzoylalanine are measured using a buffered mobile phase. Knowing the amount of BSA immobilized on the column (36 mg), the ratio of the number of enantiomer molecules needed to saturate the enantioselective retention mechanism to the number of BSA molecules is determined. The mean of the set of eight enantiomers is 0.28. These data confirm that at most one enantioselective site exists for each BSA molecule for the kind of enantiomers studied.
在一根硅胶柱上共价固定了牛血清白蛋白（BSA），使用缓冲流动相测量了扁桃酸、色氨酸、2-苯基丁酸和N-苯甲酰丙氨酸对映体的吸附等温线。已知固定在柱上的BSA量（36毫克），确定了使对映选择性保留机制饱和所需的对映体分子数与BSA分子数的比率。所研究的八种对映体的该比率平均值为0.28。这些数据证实，对于所研究的这类对映体，每个BSA分子最多存在一个对映选择性位点。
