Nishiyama Y, Nakayama S, Okada Y, Min K S, Onosaka S, Tanaka K
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.
Chem Pharm Bull (Tokyo). 1990 Aug;38(8):2112-7. doi: 10.1248/cpb.38.2112.
A pentacosapeptide corresponding to the entire amino acid sequence of Agaricus bisporus metallothionein (MT) and related cysteine-containing peptides were prepared by the conventional solution method and their heavy metal-binding properties were examined. The Cu2(+)- or Cu(+)-binding activities of various peptides were not greatly dependent on the peptide structure, so far as examined, although the pentacosapeptide, A. bisporus MT, exhibited slightly higher binding activity than the other peptides. On the contrary, the Cd2(+)-binding activities of these peptides were fairly structure-dependent.
通过传统溶液法制备了与双孢蘑菇金属硫蛋白(MT)的完整氨基酸序列相对应的二十五肽以及相关含半胱氨酸肽,并对它们的重金属结合特性进行了研究。就所检测的情况而言,各种肽对Cu2(+)或Cu(+)的结合活性在很大程度上不依赖于肽的结构,尽管二十五肽双孢蘑菇MT的结合活性略高于其他肽。相反,这些肽对Cd2(+)的结合活性则相当依赖于结构。