对从牛链球菌中分离出的粘肽结构的化学研究。
Chemical studies on the structure of mucopeptide isolated from Streptococcus bovis.
作者信息
Kane J, Lackland H, Karakawa W W, Krause R M
出版信息
J Bacteriol. 1969 Jul;99(1):175-9. doi: 10.1128/jb.99.1.175-179.1969.
Abstract
Mucopeptides isolated from Streptococcus bovis cell walls were found to be composed of alanine, glutamic acid, lysine, and threonine in a mole ratio of 3:1:1:1. A dipeptide, N(epsilon)-lysylthreonine, was isolated from S. bovis mucopeptide by ion-exchange chromatography. This finding suggests that threonine is associated with the bridge which cross-links adjacent tetrapeptides by connecting the epsilon-amino group of lysine of one tetrapeptide to the carboxyl group of d-alanine of another to form the mucopeptide matrix.
摘要
从牛链球菌细胞壁分离出的粘肽被发现由丙氨酸、谷氨酸、赖氨酸和苏氨酸组成，摩尔比为3:1:1:1。通过离子交换色谱法从牛链球菌粘肽中分离出一种二肽，N(ε)-赖氨酰苏氨酸。这一发现表明，苏氨酸与通过将一个四肽的赖氨酸的ε-氨基连接到另一个四肽的d-丙氨酸的羧基上，从而交联相邻四肽的桥有关，以形成粘肽基质。
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