1992 年 40 巻 10 号 p. 2701-2706
A nonacosapeptide corresponding to the N-terminal sequence 1-29 (β-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 Cd2+-binding activities of these peptides were fairly structure-dependent.