氨基酸与肽。三十三。哺乳动物金属硫蛋白（MTs）N端表位肽的合成。

Amino acids and peptides. XXXIII. Synthesis of N-terminal epitope peptides of mammalian metallothioneins (MTs).

作者信息

Okada Y, Nakayama S, Iguchi S, Kikuchi Y, Irie M, Sawada J, Ikebuchi H, Terao T

机构信息

Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.

出版信息

Chem Pharm Bull (Tokyo). 1992 Apr;40(4):1029-32. doi: 10.1248/cpb.40.1029.

DOI:10.1248/cpb.40.1029

PMID:1381995

Abstract

In order to determine the fine structure of the mammalian metallothionein (MT) epitope to a monoclonal anti-rat Zn-MT-II antibody (MT 189-14-7), N-terminal peptides of various lengths of mammalian metallothioneins (MTs) were synthesized by a conventional solution method using the newly developed beta-2-adamantylaspartate, and their immunological properties were examined. It was found that the N-terminal acetyl group was indispensable for the reaction with the monoclonal antibody and the N-terminally acetylated pentapeptide, Ac-Met-Asp-Pro-Asn-Cys-OH, was the smallest peptide which exhibited a significant reactivity with the antibody.

摘要

为了确定哺乳动物金属硫蛋白（MT）表位针对单克隆抗大鼠锌-MT-II抗体（MT 189-14-7）的精细结构，使用新开发的β-2-金刚烷天冬氨酸，通过传统溶液法合成了各种长度的哺乳动物金属硫蛋白（MTs）的N端肽，并检测了它们的免疫特性。发现N端乙酰基对于与单克隆抗体的反应是必不可少的，并且N端乙酰化的五肽Ac-Met-Asp-Pro-Asn-Cys-OH是与该抗体表现出显著反应性的最小肽。