摘要
本文建立了一种新的方法──微透析法用于研究金属离子铺与人血清蛋白（Ｈｕｍａｎ Ｓｅｒｕｍ Ａｌｂｕｍｉｎ，简称ＨＳＡ）的相互作用．测定了金属离子Ｃｄ２＋与ＨＳＡ之间的结合位点数为１．８１和结合常数３．５５×１０５Ｍ－１微透析回收率Ｃｄ２＋为５８．３６％（Ｒ．Ｓ．Ｄ２．１％，ｎ＝６）．通过各种离子之间的竞争结合建立了通用的判定金属离子的共同结合位点及相对结合强度的方法．证明在ＨＳＡ上Ｃｄ２＋和Ｚｎ２＋有共同的第一结合位点，它们在ＨＳＡ上有一多元素的共同结合位点．应用本实验方法可以节约蛋白３／４以上，并具有精确、快速、方便等特点．
In this paper, a new method-micrdialysis has been established to determine the interaction binding parameters of Cd2+ with human serum albumin (HSA). The recoveries of meta1 ions on microdialysis are Zn2+ 70.45% (RSD of 3.2%, n=6) and Cd2+ 58.36% (RSD 2.1%, n=6). The primary binding numbers and constants are: 1.81 and 3.55×105M-1 for Cd2+. Through competing binding experiments of these metal ions on HSA a way of judging the common binding sites and relative binding strength has been established. There is a common primary binding site of Cd2+ and Zn2+ on HSA. There is a common second binding site of mu1tip1e meta1 ions on HSA. Using this precise, quick and convenient method more than 3/4 protein can be saved.
出处
《大连大学学报》
2001年第6期7-12,26,共7页
Journal of Dalian University
基金
国家自然科学基金资助项目(20141009)
关键词
微透析法
金属离子
镉
人血清蛋白
HSA
生物无机化学
microdialysis
high performance liquid chromatography, human serum albumin,cadmium, bind
