胶原蛋白交联的化学性质。可还原中间交联的稳定机制。
The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links.
作者信息
Robins S P, Bailey A J
出版信息
Biochem J. 1975 Aug;149(2):381-5. doi: 10.1042/bj1490381.
Abstract
The periodate-degradation technique was used to demonstrate the mechanism by which the reducible cross-links of collagen are stabilized. In all the tissues examined, Smith degradations of the 3H-labelled cross-links indicated that dihydroxylysinonorleucine is derived solely from hydroxylysino-5-oxonorleucine, the Amadori-rearranged product of the original condensation reaction. Monohydroxylysinonorleucine exists in both keto and aldimine forms, the former being derived from hydroxyallysine and the latter from allysine. Their relative proportions are tissue-dependent and are related to the degree of hydroxylation of the specific lysine residues in both the telopeptides and the triple helix.
摘要
采用高碘酸盐降解技术来证明胶原蛋白可还原交联得以稳定的机制。在所有检测的组织中，对3H标记交联物进行的史密斯降解表明，二羟基赖氨酰正亮氨酸仅来源于羟赖氨酰-5-氧代正亮氨酸，即原始缩合反应的阿马多里重排产物。单羟基赖氨酰正亮氨酸以酮式和醛亚胺式两种形式存在，前者来源于羟烯赖氨酸，后者来源于烯赖氨酸。它们的相对比例因组织而异，并且与端肽和三螺旋中特定赖氨酸残基的羟基化程度有关。
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