一种表层水鱼类康氏马鲛皮肤胶原蛋白的特性分析。

Characterization of the skin collagen of a surface water fish Scomberoides commersonianus.

作者信息

Nagamalleswari D, Joseph K T

机构信息

Biochemistry Department, Central Leather Research Institute, Adyar, Madras, India.

出版信息

Biochem Int. 1991 Aug;24(6):1063-73.

PMID:1781785

Abstract

The molecular organization of the skin collagen in the fish S. commersonianus has been investigated. The contents of imino acids proline and hydroxyproline are less in the skin collagen. The major collagenous component of fish skin is homologous to type I collagen. The number of CNBr peptides in fish skin collagen alpha 1 chains is two times that of rat skin alpha 1 CNBr peptides. The proline-hydroxyproline ratio in the six peptides studied was 1.66-3.5 as compared to that of rat skin collagen (0.67-1.94). This indicates that proline and hydroxyproline are not uniformly distributed in the collagen molecule in fish skin collagen.

摘要

已对康氏南美南极鱼（Stephanolepis commersonianus）皮肤胶原蛋白的分子结构进行了研究。该鱼皮肤胶原蛋白中亚氨基酸脯氨酸和羟脯氨酸的含量较少。鱼皮的主要胶原成分与I型胶原蛋白同源。鱼皮胶原蛋白α1链中CNBr肽的数量是大鼠皮肤α1 CNBr肽数量的两倍。在所研究的六种肽中，脯氨酸与羟脯氨酸的比例为1.66至3.5，而大鼠皮肤胶原蛋白的该比例为0.67至1.94。这表明在鱼皮胶原蛋白的胶原分子中，脯氨酸和羟脯氨酸并非均匀分布。