摘要
研究了金属离子与血清蛋白形成配合物的条件,探讨了用金属离子-蛋白质配合物消除毛细管区带电泳中管壁吸附作用的方法,并将之成功应用于人血清中药物成分的分离。试验证明,血清蛋白与多种金属离子能不同程度地形成配合物,除Mg2+外,所选金属离子与血清蛋白形成配合物的优先顺序为Zn2+>Cu2+>Cd2+>Co2+>Fe3+>Cr3+>Mn2+>Ca2+>Ni2+;配合物的稳定性取决于介质的pH、温度和金属离子的浓度,其适宜范围分别为pH=6～8,温度40～50℃,金属离子浓度10～30mg/L;金属离子与蛋白质的作用有效地解决了管壁吸附问题,铜和锌离子-蛋白质配合物既不影响药物成分的分离,也不降低毛细管分离效能;分离血清中药物成分的图谱基线稳定,各成分的迁移时间在连续3周的多次实验中重复性好,相对标准偏差在0.14%～0.36%。
This paper studied the reaction condition of metal ions with human serum protein by atomic absorption spectrometry,discussed method of eliminating the absorption of protein on the wall of capillary tube,and successfully applied it to separate medical compound in human serum.It was proved that except Mg 2+ ,serum protein could form metal protein complex with several metal ions and the order was Zn 2+ >Cu 2+ >Cd 2+ >Co 2+ >Fe 3+ >Cr 3+ >Mn 2+ >Ca 2+ >Ni 2+ .Stability of the complex depended on medium pH,temperature and ion concentration.The suitable ranges were pH=6-8,temperature 40-50 ℃,ion concentration 10 ～30 mg/L.It was separated by capillary zone electrophoresis by adding either copper or zinc ions,which was most efficient among the metals into acidified human serum samples spiked with some medical compounds.The electrophoretograms showed that baseline was stable,and no absorption was observed during three weeks day to day experiments,the repeatability of mobile time with each compoud was good,RSD between 0.14%-0.36%.
出处
《西北农林科技大学学报（自然科学版）》
CSCD
北大核心
2005年第5期100-104,共5页
Journal of Northwest A&F University(Natural Science Edition)
关键词
金属离子
血清蛋白质
毛细管电泳
药物成分
metals
serum proteins
capillary electrophoresis
medical compounds
