Some Properties of Collagen form the Abalone.
Some Properties of Collagen form the Abalone.
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鲍鱼中胶原蛋白的一些特性。
DOI：
10.2331/suisan.34.925
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发表时间：
1968
影响因子：
0.4
通讯作者：
M. Kubota
中科院分区：
文献类型：
--
作者：
S. Kimura;M. Kubota
为了研究贝类胶原蛋白，对皱纹盘鲍鲍体进行了分离，并对其氨基酸组成和一些物理性质进行了表征。胶原蛋白含量在20%左右，足部胶原蛋白含量丰富，足部是运动器官。由于大部分胶原蛋白不溶于中性盐或稀酸，不溶性胶原蛋白被胃蛋白酶增溶。通过加入NaCl至终浓度为5%使胃蛋白酶溶解的胶原蛋白（PSC）沉淀，并再溶解于0.01 N HCl中。PSC的特性粘度和旋光度的值与脊椎动物胶原蛋白，如哺乳动物或鱼皮胶原蛋白的相似，但在氨基酸组成中发现了明显的差异。PSC富含酸性氨基酸、酰胺、羟基赖氨酸和酪氨酸，但缺乏甘氨酸、丙氨酸和组氨酸。变性温度（Td：22.5 ° C，pH 2）和总亚氨基酸含量（181.3残基/1000）的值就这两个值之间的关系而言显示出与普通胶原的良好一致性。最大的特征之一是赖氨酸的进一步羟基化。胶原蛋白中羟赖氨酸的含量大于赖氨酸的含量，因此赖氨酸与羟赖氨酸的比值约为0.6，而脊椎动物胶原蛋白的比值为3 - 5。此外，PSC含有少量胱氨酸（2.8个残基/1000）和大量己糖（2.2%）。氨基酸组成中的这些特征与Piez等人报道的其他无脊椎动物胶原蛋白（Metridium和Thyone）中的发现相对应。从这些结果可以推测，鲍鱼体内的胶原蛋白在分子结构上与脊椎动物胶原蛋白相似，但氨基酸组成不同。
In order to investigate the shellfish collagen, the body of abalone, Haliotis discus, was isolated and characterized with respect to the amino acid composition and some physical properties. The collagen content of the body was about 20% and was rich in foot part which plays the role of locomotive organ. As most of the collagen was insoluble in neutral salts or dilute acids, the insoluble collagen was solubilized by pepsin. The pepsin solubilized collagen (PSC) was precipitated by addition of NaCl to a final concentration of 5% and redissolved in 0.01 N HCl. The values of intrinsic viscosity and optical rotation of the PSC were similar to those of vertebrate collagens, such as mammalian or fish skin collagens, but distinct differences were found in the amino acid composition. The PSC was rich in acidic amino acids, amide, hydroxylysine, and tyrosine, but poor in glycine, alanine, and histidine. The values of denaturation temperature (Td: 22.5°C at pH 2) and total imino acids content (181.3 residue/1000) showed a good agreement with usual collagens with respect to the relationship between these two values. One of the most characteristics is a further hydroxylation of lysine. The content of hydroxylysine was larger than that of lysine, thus the ratio of lysine to hydroxylysine was about 0.6, comparing with 3-5 for vertebrate collagens. Moreover, the PSC contained a small amount of cystine (2.8 residues/1000) and a considerable amount of hexose (2.2%). These characteristics in amino acid composition corresponded with the finding in other invertebrate collagens, Metridium and Thyone, reported by Piez et al. From these results, it is assumed that the collagen from the body of abalone is similar to vertebrate collagens in its molecular structure, but not in amino acid composition.