CHEMISTRY OF THE COLLAGEN CROSS-LINKS - ORIGIN AND PARTIAL CHARACTERIZATION OF A PUTATIVE MATURE CROSS-LINK OF COLLAGEN
CHEMISTRY OF THE COLLAGEN CROSS-LINKS - ORIGIN AND PARTIAL CHARACTERIZATION OF A PUTATIVE MATURE CROSS-LINK OF COLLAGEN
复制标题
DOI：
10.1042/bj2440303
复制
发表时间：
1987-06-01
影响因子：
4.1
通讯作者：
BAILEY, AJ
中科院分区：
文献类型：
--
作者：
BARNARD, K;LIGHT, ND;BAILEY, AJ
胶原中可还原的二价交联转化为成熟胶原中不可还原的多价交联，导致鉴定出几种新的氨基酸作为假定的成熟交联。这些化合物都没有完全满足必要的标准。我们现在已经分离出一种高Mr的氨基酸，来源于赖氨酸，这种氨基酸只存在于来源于成熟胶原蛋白的高Mr肽中。它随着组织年龄的增长而增加，与可还原性交联的减少相关，并且它存在于成熟的皮肤和骨骼中，它们最初分别通过醛二胺和氧亚胺二价交联进行交联。我们提出，这种氨基酸，尚未完全表征和指定的化合物M，是成熟胶原蛋白的主要交联。
The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.