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肾形软骨海绵胶原蛋白的增溶与特性分析

Solubilization and characterization of Chondrosia reniformis sponge collagen.

作者信息

Imhoff J M, Garrone R

出版信息

Connect Tissue Res. 1983;11(2-3):193-7. doi: 10.3109/03008208309004855.

DOI:10.3109/03008208309004855
PMID:6309474
Abstract

Chondrosia reniformis sponge collagen, insoluble in its native form, was solubilized by chemical modification of lysyl residues. The solubilized sponge collagen had the same amino acid composition as insoluble collagen and the helicoidal tertiary structure was found by negative Cotton effect to be the same as in native vertebrate collagens. Achromobacter iophagus collagenase, a collagen specific protease, hydrolyzed the soluble sponge collagen. These experiments confirmed that the protein had the same structure as collagen.

摘要

肾形软骨海绵胶原蛋白以其天然形式不溶,通过对赖氨酰残基进行化学修饰而溶解。溶解后的海绵胶原蛋白与不溶性胶原蛋白具有相同的氨基酸组成,通过负科顿效应发现其螺旋三级结构与天然脊椎动物胶原蛋白相同。食菌无色杆菌胶原酶是一种胶原特异性蛋白酶,可水解可溶性海绵胶原蛋白。这些实验证实该蛋白质具有与胶原蛋白相同的结构。

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