甜味抑制多肽奇果菌素中二硫键的位置

Location of the disulfide bonds of the sweetness-suppressing polypeptide gurmarin.

作者信息

Ota M, Ariyoshi Y

机构信息

Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.

出版信息

Biosci Biotechnol Biochem. 1995 Oct;59(10):1956-7. doi: 10.1271/bbb.59.1956.

DOI:10.1271/bbb.59.1956

PMID:8534991

Abstract

The sweetness-suppressing polypeptide gurmarin has been isolated from the leaves of Gymnema sylvestre and consists of 35 amino acid residues including three intramolecular disulfide bonds. The primary structure has already been determined. The positions of the disulfide bonds were located, by a combination of mass spectrometric analysis and sequencing of cystine-containing peptides obtained by thermolysin-catalyzed hydrolysis of gurmarin, to be at Cys3-Cys18, Cys10-Cys23, and Cys17-Cys33.

摘要

甜味抑制多肽匙羹藤酸已从匙羹藤的叶子中分离出来，它由35个氨基酸残基组成，包括三个分子内二硫键。其一级结构已经确定。通过质谱分析和对嗜热菌蛋白酶催化水解匙羹藤酸所得含胱氨酸肽段的测序相结合，确定二硫键的位置为Cys3-Cys18、Cys10-Cys23和Cys17-Cys33。