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鲨鱼I型胶原蛋白的结构特性及体外自组装

Structural property and in vitro self-assembly of shark type I collagen.

作者信息

Nomura Y, Yamano M, Hayakawa C, Ishii Y, Shirai K

机构信息

Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan.

出版信息

Biosci Biotechnol Biochem. 1997 Nov;61(11):1919-23. doi: 10.1271/bbb.61.1919.

Abstract

The main structure of shark type I collagen is similar to that of land mammals, with a partial difference in amino acid sequence and post-translational modification. By static light scattering, the weight-average molecular weight of shark collagen (7.52 x 10(5)) suggests the presence of some aggregated molecules, oligomeric collagen. The self-assembly curve of shark collagen had a shorter lag phase and a longer growth phase than that of pig collagen. The optimum temperature and pH of shark collagen self-assembly is different from that of pig collagen.

摘要

鲨鱼I型胶原蛋白的主要结构与陆地哺乳动物的相似,但在氨基酸序列和翻译后修饰方面存在部分差异。通过静态光散射,鲨鱼胶原蛋白的重均分子量(7.52×10⁵)表明存在一些聚集分子,即寡聚胶原蛋白。鲨鱼胶原蛋白的自组装曲线与猪胶原蛋白相比,滞后相较短,生长相较长。鲨鱼胶原蛋白自组装的最佳温度和pH与猪胶原蛋白不同。

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