Amino acids and peptides. XXVI. Synthesis of Agaricus bisporus metallothionein and related peptides and examination of their heavy metal-binding properties.
pentacosapeptide corresponding to the entire aminoacid 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
The common N-terminal heptapeptide, Ac-Met-Asp-Pro-Asn-Cys-Ser-Cys-OH, Ac-(MT II 1-7)-OH, of mammalian metallothioneins (MTs) was synthesised by a conventional solution method using newly developed β-2-adamantylasparate. This peptide was as reactive as native MT with a monoclonal antibody produced against rat Zn-MT II.
哺乳动物金属硫蛋白(MTs)的共同N端七肽Ac-Met-Asp-Pro-Asn-Cys-Ser-Cys-OH,即Ac-(MT II 1-7)-OH,通过使用新开发的β-2-金刚烷基天冬氨酸,采用传统的溶液方法合成。该肽与针对大鼠Zn-MT II产生的单克隆抗体同样具有反应性。