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氧化交联稳定在食物剥夺大鼠中胶原蛋白聚合增加中的作用。

The role of oxidative cross-link stabilization in increased collagen polymerization in food deprived rats.

作者信息

Deyl Z, Macek K

出版信息

Physiol Bohemoslov. 1982;31(6):537-42.

PMID:6219409
Abstract

It was demonstrated that 50% food restriction for a period of two years causes a considerable increase in gamma-chain polymers of rat skin collagen. The polymerization reaction occurs in both main skin collagen types, e.g. collagen type I and III. Concomitantly increased amounts of alpha-aminoadipic acid were found in preparations of food deprived rats as compared to the controls. It appears that this unusual amino acid arises from the oxidative stabilization of dehydro hydroxylysinonorleucine, the main intermolecular collagen cross-link present in the skin. It is suggested that the degree of polymerization of skin collagen in fasted animals is the result of reutilization of more soluble collagen forms.

摘要

结果表明,持续两年50%的食物限制会使大鼠皮肤胶原蛋白的γ链聚合物显著增加。聚合反应发生在两种主要的皮肤胶原蛋白类型中,即I型和III型胶原蛋白。与对照组相比,在食物缺乏大鼠的制剂中发现α-氨基己二酸的含量也相应增加。这种不寻常的氨基酸似乎来自脱氢羟赖氨酰正亮氨酸的氧化稳定化,后者是皮肤中主要的分子间胶原蛋白交联物。有人认为,禁食动物皮肤胶原蛋白的聚合程度是更易溶的胶原蛋白形式再利用的结果。

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