Abstract
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.

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