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胶原蛋白交联的化学性质。体内脱氢赖氨酸正亮氨酸和脱氢羟赖氨酸正亮氨酸未发生还原反应。

The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo.

作者信息

Bailey A J, Peach C M

出版信息

Biochem J. 1971 Jan;121(2):257-9. doi: 10.1042/bj1210257.

Abstract

Two aldimine bonds have been shown to be present as stabilizing cross-links in intact collagen fibres from soft tissues: dehydrohydroxylysinonorleucine as a major component and dehydrolysinonorleucine being present in trace quantities. In the highly insoluble collagens less dehydrohydroxylysinonorleucine is present but the proportion of dehydrolysinonorleucine increases. In elastin the latter aldimine is reduced in vivo to give a more stable cross-link but no comparable reduction could be detected with either of the aldimines present in collagen.

摘要

已证明在来自软组织的完整胶原纤维中存在两种醛亚胺键作为稳定的交联键

脱氢羟赖氨酸正亮氨酸是主要成分,脱氢赖氨酸正亮氨酸以痕量存在。在高度不溶性胶原中,脱氢羟赖氨酸正亮氨酸的含量较少,但脱氢赖氨酸正亮氨酸的比例增加。在弹性蛋白中,后一种醛亚胺在体内被还原以形成更稳定的交联,但在胶原中存在的任何一种醛亚胺中均未检测到类似的还原。

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Isolation of lysinonorleucine from collagen.从胶原蛋白中分离赖氨酰正亮氨酸。
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