【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α HLA抗变性剂和热诱导的去折叠性能更多还原

【Abstract】 Affinity 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.更多还原