A nonacosapeptide corresponding to the N-terminal sequence 1—29 (β-fragment) of human liver metallothionein II (hMT II) was synthesized by the azide coupling of five peptide fragments [1, 2, 4, 6 and 8], followed by HF deprotection and its heavy metal-binding properties were examined. It was revealed that the Cd-binding ability of the synthetic β-fragment as well as synthetic α-fragment corresponding to the C-terminal sequence 30—61 of hMT II was stronger than that of native rat thionein. Moreover, it was found that both the α- and β-fragments bound preferentially to Cu ions rather than Cd ions. © 1986, The Pharmaceutical Society of Japan. All rights reserved.
CITATION STYLE
Okada, Y., Min, K. S., Ohta, N., Onosaka, S., Iguchi, S., Tanaka, K., … Yagyu, M. (1986). Amino Acids and Peptides. XIII. Synthesis of a Nonacosapeptide Corresponding to the N-Terminal Sequence 1—29 (β-Fragment) of Human Liver Metallothionein II (hMT II) and Its Heavy Metal-Binding Properties. Chemical and Pharmaceutical Bulletin, 34(3), 986–998. https://doi.org/10.1248/cpb.34.986
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