Okada Y, Ohta N, Yagyu M, Min K S, Onosaka S, Tanaka K
FEBS Lett. 1985 Apr 22;183(2):375-8. doi: 10.1016/0014-5793(85)80813-9.
A nonacosapeptide (beta-fragment) corresponding to the N-terminal sequence 1-29 of human liver metallothionein II was synthesized by the fragment condensation method. The Cd-binding ability of the beta-fragment was much stronger than that of cysteine as thionein and synthetic alpha-fragment corresponding to the C-terminal sequence 30-61 of human liver metallothionein II. Both the alpha- and beta-fragments bound preferentially to Cu ions rather than Cd ions.
通过片段缩合方法合成了一种与人类肝脏金属硫蛋白II的N端序列1 - 29相对应的二十九肽(β片段)。该β片段与半胱氨酸作为硫蛋白以及与人类肝脏金属硫蛋白II的C端序列30 - 61相对应的合成α片段相比,其结合镉的能力要强得多。α片段和β片段都优先结合铜离子而非镉离子。