Chemical Synthesis of a Heat-stable Enterotoxin of<i>Yersinia enterocolitica</i>
作者:Shoko Yoshimura、Yasutsugu Shimonishi
DOI:10.1246/bcsj.58.2805
日期:1985.10
A peptide with the amino acid sequence Ser–Ser–Asp–Trp–Asp–Cys–Cys–Asp–Val–Cys–Cys–Asn–Pro–Ala–Cys–Ala–Gly–Cys of heat-stable enterotoxin (ST) produced by Yersinia enterocolitica was synthesized by a conventional method. The synthetic peptide was found to be identical with the corresponding natural peptide by chemical and physicochemical criteria, thus establishing the amino acid sequence of an ST of Yersinia enterocolitica.
Amino Acids and Peptides. XXXIV. Synthesis of Mouse Metallothionein I.(1). Synthesis of Dotriacontapeptide Corresponding to C-Terminal Sequence 30-61 (.ALPHA.-Fragment) of Mouse Metallothionein I and Related Peptides and Examination of Their Heavy Metal-Binding Properties.
The dotriacontapeptide corresponding to the C-terminal sequence of mouse metallothionein (MT) I and related peptides which contain Cys-X-Cys-Cys (X : amino acid residue except for Cys) sequence were synthesized by the conventional solution method employing the HF deprotection method and their heavy metals (Cd2+, Cu2+ and Cu+)-binding properties were examined.
合成了对应于小鼠金属硫蛋白 (MT) I C末端序列的三十二肽及相关肽,这些肽包含Cys-X-Cys-Cys(X:除Cys外的氨基酸残基)序列,采用传统溶液法结合HF去保护法,并对它们与重金属(Cd2+、Cu2+和Cu+)的结合特性进行了研究。