A C-terminal hexacosapeptide corresponding to residues 36-61 of human liver metallothionein (hMT II) was synthesized by the fragment condensation method using the azide procedure. Protecting groups were removed by the methanesulfonic acid (MSA) method or hydrogen fluoride (HF) method to give the desired peptide. The binding ability of this peptide with Cd and Zn was examined by measuring the absorbance in the ultraviolet region (200-260 nm) as a function of heavy metal concentration and by the gel-filtration method. The heavy metal-binding behavior of this peptide is quite similar to that of thionein.
使用
叠氮化物程序通过片段缩合法合成了对应于人肝
金属
硫蛋白(h
MT II)的残基36-61的C端六肽。通过
甲磺酸(M
SA)法或
氟化氢(HF)法去除保护基,得到所需的肽。通过测量紫外区(200-260 nm)的吸光度作为重
金属浓度的函数并通过凝胶过滤方法检查该肽与 Cd 和 Zn 的结合能力。该肽的重
金属结合行为与
硫因非常相似。