【摘要】 <正> 金属硫蛋白（Metallothionein,简称MT）是一类低分子量（哺乳动物MT的分子量为6500）、富含半胱氨酸（一般占氨基酸残量的30％）且具有高度可诱导性的金属结合蛋白。关于其结构与功能的研究是当今化学、生物学和临床医学等领域的重要课题之一。但是,有关各种生物MTs水溶液的热力学稳定性的研究尚未见报道。本文通过对在pH 7.40、4℃下放置不同时间的家兔肝脏（Cd,zn）₇MT水溶液进行HPLC分离,首次观察到MT在水溶液中的缓慢聚合现象,得到聚合反应的表观二级反应速率常数,发现MT-2比MT-1更易聚合。更多还原

【Abstract】 Chromatographic separation of the aqueous solutions of rabbit hepatic (Cd,Zn)7MT in 50 mmol/L sodium phosphate (pH 7. 40) after storing for various time was performed on HPLC in an attempt to investigate the thermodynamic stability of the Metallothionein (MT) solution. It was found that MT could polymerize slowly by itself. Assuming the polymerization only occurs from monomer to dimer, an apparent bimolecular rate constant of the order of 10-3(mol/L)-1·/day-1 at 4℃ was obtained. The results also clearly reveal that the isoform MT-2 can polymerize more easily than MT-1.更多还原