Ca^(2+)与乳清蛋白结合的亲和毛细管电泳研究  

Study on Human α-Lactalbumin-Calcium Interaction Using Affinity Capillary Electrophoresis

作　　者：王畅[1] 郑育芳[1] 熊建辉[1] 翁前锋[1] 杨军[1] 杨青[1] 许国旺[1] 

机构地区：[1]中国科学院大连化学物理研究所国家色谱分析中心,大连116011

出　　处：《化学学报》2004年第3期279-282,共4页Acta Chimica Sinica

基　　金：中国科学院领域前沿创新基金 (Nos.K2 0 0 2A1 1 ;K2 0 0 2A1 2 )资助项目

摘　　要：利用亲和毛细管电泳研究了Ca2 + 与α 人乳清蛋白 (α HLA)的结合情况 .以恒定浓度α HLA作为受体 ,运行缓冲溶液加入不同浓度的Ca2 + 作为配体 ,可观察到由于Ca2 + 的结合 ,α HLA的电泳淌度发生了变化 .通过Scatchard方程的淌度比(M)处理数据得到α HLA与Ca2 + 的表观结合常数 (Kapp)为 2 0× 10 7(mol/L) -1.同时考察了Ca2 + 对变性剂 (尿素 )和热诱导所引起的α HLA去折叠的影响 ,结果表明 ,Ca2 + 的结合增强了α HLA的稳定性 ,也即提高了αAffinity capillary electrophoresis was used to study the interaction of human α-lactalbumin (α-HLA) with calcium ion(Ca 2+). With constant concentration of α-HLA as a receptor and various concentrations of Ca 2+ as a ligand in the running buffer, changes in electrophoretic mobilities of α-HLA were observed when complexes of α-HLA and Ca 2+came into being. Based on Scatchard analysis of the mobility ratios (M) of α-HLA to Ca 2+, it was found that the apparent binding constant (K app) was 2.0×10 7(mol/L) -1. In addition , the effect of Ca 2+ on the unfolding of α-HLA induced by urea and heating was studied, and the results showed that the binding of Ca 2+ increased the stability of α-HLA against the action of denaturing agent (such as urea) and heating.

关 键 词：乳清蛋白 钙离子 亲和毛细管电泳 结合作用 淌度 乳糖合成 去折叠性能 

分 类 号：O658.9[理学—分析化学]