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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。胶原的成熟推定交联的起源和部分表征。

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摘要

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.
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不可还原的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标准。现在我们已经分离出了赖氨酸的高Mr氨基酸,这种氨基酸仅存在于成熟胶原蛋白的高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。我们建议,该氨基酸,尚未完全表征和命名为化合物M,是成熟胶原蛋白的主要交联。

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