CAJ | 학술논문

采用三聚氯氰为活化剂分别合成了牛血清白蛋白（BSA）、人血清白蛋白（HSA）和β-环糊精手性固定相，研究了温度在色氨酸,华法令，酮基布洛芬和丹酰化苏氨酸手性拆分中的影响。结果表明，在蛋白手性固定相上对映体间的熵变对色氨酸,华法令和酮基布洛芬的拆分有很大的影响，而丹酰化苏氨酸对映体在β-环糊精手性固定相上的拆分为典型的焓控过程，与蛋白柱有着不同的热力学特性。由于键合方式不同，色氨酸在我们合成的BSA手性固定相上的最佳分离温度为35℃左右，而不是文献报道的以戊二醛为活化剂的24℃。
채용삼취록청위활화제분별합성료우혈청백단백（BSA）、인혈청백단백（HSA）화β-배호정수성고정상，연구료온도재색안산,화법령，동기포락분화단선화소안산수성탁분중적영향。결과표명，재단백수성고정상상대영체간적적변대색안산,화법령화동기포락분적탁분유흔대적영향，이단선화소안산대영체재β-배호정수성고정상상적탁분위전형적함공과정，여단백주유착불동적열역학특성。유우건합방식불동，색안산재아문합성적BSA수성고정상상적최가분리온도위35℃좌우，이불시문헌보도적이무이철위활화제적24℃。
The effect of column temperature on enantiomeric resolution s oftryptophan, warfarin and ketoprofen was investigated on bovine and human serum albumin (BSA and HSA) stationary phases, which were synthesized with s-triazine as the activator. It was observed that the e ntropy change made a great contribution to the separation of those enantiomers o n albumin chiral stationary phases. The column temperature for the maximal resol ution of tryptophan on the BSA stationary phase prepared by this method was abou t 35 ℃, which was not 24 ℃ as reported for the BSA stationary phase sy n thesized with glutaric dialdehyde as the activator. This results may come from the different conformation of the immobilized BSA and HSA due to the different c oupling methods used. On the other hand, it was indicated that the resolution of enantiomers on β -CD chiral stationary phase was mainly contributed from the change of enthalp y, which means the resolution of chiral solutes on albumin and β-CD statio nary phases has different thermodynamic behaviors.