Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas
Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas
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DOI：
10.1016/s0141-8130(03)00054-0
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发表时间：
2003-09-01
影响因子：
8.2
通讯作者：
Mann, S
中科院分区：
文献类型：
--
作者：
Ikoma, T;Kobayashi, H;Mann, S
从大花鱼和尼罗罗非鱼的鱼鳞中提取I型胶原蛋白，可能是一种未被充分利用的药用资源。对鱼鳞进行脱盐处理。用EDTA和胃酶消化。合成的I型胶原蛋白含有33.6%以上的甘氨酸作为最丰富的氨基酸。两种胶原蛋白的变性温度分别为303K和308K，均低于猪真皮胶原的变性温度(314K)。圆二色谱表明，变性温度取决于羟基脯氨酸的量，而不是脯氨酸残基。拉曼光谱还表明，由于亚氨基酸的含量不同，分配给Hyp和Pro环的879和855 cm(-1)处的拉曼线的相对强度也发生了变化。值得注意的是，鱼鳞中含硫蛋氨酸的含量高于猪真皮。热分析得到的热焓和熵可以与I型胶原的氨基酸序列(Gly-Pro-Hyp)和蛋氨酸氨基酸残基的数量相关联。(C)2003爱思唯尔B.V.保留所有权利。
Type I collagens were extracted from fish scales of Pagrus major and Oreochromis niloticas as a possible underutilized resource for medical materials. The fish scales were demineralized. with EDTA and digested by pepsin. The resultant type I collagens contained more than 33.6% of glycine as the most abundant amino acid. The denaturation temperatures of the collagens from P. major and O. niloticas were 303 and 308 K, respectively, both of which were relatively lower than that of porcine dermis collagen (314 K). CD spectra indicated that the denaturation temperatures were dependent on the amount of hydroxyproline, rather than proline residues. Raman spectra also indicated that the relative intensities of Raman lines at 879 and 855 cm(-1) assigned to Hyp and Pro rings were changed due to the contents of the imino acids. Significantly, the content of sulphur-containing methionine was higher in the fish scales than in porcine dermis. The enthalpy and entropy estimated from thermal analyses could be correlated to amino acid sequences (Gly-Pro-Hyp) of type I collagens and the number of methionine amino acid residues. (C) 2003 Elsevier B.V. All rights reserved.