金属硫蛋白的提纯  

Purification of Metallothionein

作　　者：张亨山[1] 赵金垣[1] 陈晓龙[2] 张振龙[2] 王春荣[2] 倪道明[2] 史德林[2] 黄文萱 刘宏 马东星[4] 

机构地区：[1]北京医科大学第三医院 [2]卫生部北京生物制品研究所 [3]大同医专 [4]武警总医院

出　　处：《大同医学专科学校学报》1999年第4期4-8,共5页Journal of Datong Medical College

基　　金：国家自然科学基金

摘　　要：金属硫蛋白(MT)是一类广泛分布、富含半胱氨酸,可结合金属的低分子量非酶蛋白质。它在金属中毒、微量元素代谢调节和抗射线、自由基损伤等方面有重要作用。本研究提纯了兔肝MT_1和MT_2(rlMT_1、rlMT_2)。方法是:先给家兔多次皮下注射CdCl_2诱导MT合成,之后取肝作匀浆,经冷乙醇提取制得MT粗提液。该粗提液通过Sepbaclx G—50 柱(4.5×95cm)和DEAE-cellulose DE52 柱(2.5×4cm)层析,使分离出rlMT_1和rlMT_2两种亚型。鉴定表明,rlMT_1和rlMT_2的分子量均约14KD,纯度为SDS—PAGE分析呈单一条带,与Sigma标准品的分子量和纯度一致。氨基酸组成中,半胱氨酸和硫基含量都接近每分子20个,不含芳香族氨基酸和组氨酸。本次研究为探寻MT检测工作,推动我国MT的研究奠定了良好基础。Metallothionein (MT) is a ubiquitous, low - mol - wt, cysteine - rich, metalbinding protein involved in resistance to metal toxity, reaction to stress, and metal homeostasis. This study made the purification for two isoforms of rabbit liver MT(rlMT1, rlMT2). The method was: rabbits were given repeated injections of Cadmium Chloride. r1MT1 and r1MT2 were obtained from the livers of these animals by precipitation procedures,SephadexG - 50 and DEAE - cellulose DE52 chromatography. The proteins thus obtained showed the purify,molecular weight,amino acid composition and suifhydryl content similar to those of Sigma standards. Therefore, a solid basis for the further study on MT functions and application was founded since then.

关 键 词：金属硫蛋白 分离纯化 

分 类 号：R[医药卫生]