Matsumoto S, Nishiyama Y, Okada Y, Min K S, Onosaka S, Tanaka K
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.
Chem Pharm Bull (Tokyo). 1992 Oct;40(10):2701-6. doi: 10.1248/cpb.40.2701.
A nonacosapeptide corresponding to the N-terminal sequence 1-29 (beta-fragment) of mouse metallothionein I and related peptides were synthesized by the conventional solution method and their heavy metals (Cu2+, Cu+ and Cd2+)-binding properties were examined. The Cu(2+)- or Cu(+)-binding activities of various peptides were not greatly dependent on the peptide structure, so far as examined, as in the cases of N. crassa MT and A. bisporus MTs. On the contrary, the Cd(2+)-binding activities of these peptides were fairly structure-dependent.
通过传统溶液法合成了与小鼠金属硫蛋白I的N端序列1-29(β片段)相对应的一种二十九肽及相关肽,并检测了它们与重金属(Cu2+、Cu+和Cd2+)的结合特性。就所检测的情况而言,各种肽的Cu(2+)或Cu(+)结合活性并不很大程度地依赖于肽结构,如同粗糙脉孢菌金属硫蛋白和双孢蘑菇金属硫蛋白的情况一样。相反,这些肽的Cd(2+)结合活性相当依赖于结构。