首页> 外文期刊>The biochemical journal >Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen
【24h】

Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen

机译:胶原蛋白的化学交联。推定的胶原蛋白成熟交联的起源和部分表征

获取原文
获取外文期刊封面目录资料

摘要

pThe 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./p
机译:>胶原蛋白中可还原的二价交联转化为成熟胶原蛋白中的不可还原多价交联已导致鉴定出几种新的氨基酸作为推定的成熟交联。这些化合物均未完全满足必要的标准。现在我们已经分离出了赖氨酸衍生的高Mr氨基酸,这种氨基酸仅存在于成熟胶原衍生的高Mr肽中。其随着组织年龄的增加而与可还原交联的减少相关,并且它存在于成熟的皮肤和骨骼中,它们最初分别通过醛亚胺和氧代亚胺二价交联而交联。我们认为,该氨基酸尚未完全鉴定并命名为化合物M,是成熟胶原蛋白的主要交联。

著录项

获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号