Characterization and subunit composition of collagen from the body wall of sea cucumber Stichopus japonicus
Characterization and subunit composition of collagen from the body wall of sea cucumber Stichopus japonicus
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DOI：
10.1016/j.foodchem.2005.11.019
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发表时间：
2007-01-01
期刊：
影响因子：
8.8
通讯作者：
Gao, Xin
中科院分区：
文献类型：
--
作者：
Cui, Feng-xia;Xue, Chang-hu;Gao, Xin
以海参（Stichopus Stichopus）体壁为原料，采用NaCl选择性沉淀法，制备了不含端肽的胃蛋白酶溶胶原蛋白（PSC）。PSC在220 nm处表现出最大吸光度。用Sephacryl S-300 HR分离纯化了PSC的亚基，SDS-PAGE结果表明，纯化的PSC胶原蛋白具有较好的生物学活性。β-淀粉样蛋白为1 α三聚体（约135 kDa），而1 α链类似于脊椎动物I型胶原的α（1）链。通过DSC测量的热稳定温度（T-s）为57.0 ℃，比小牛I型胶原蛋白的热稳定温度低约5.0 ℃。肽图和氨基酸分析也揭示了无脊椎动物和脊椎动物PSC的差异。然而，（α（1））（3）三聚体的存在是明显的。(c)2005爱思唯尔有限公司保留所有权利。
Pepsin-solubilized collagen (PSC) without telopeptides was prepared from the body wall of the sea cucumber Stichopus japonicus and isolated by selective precipitation with NaCl. The PSC exhibited a maximum absorbance at 220 nm. The subunit of PSC was isolated by Sephacryl S-300 HR. The results of SDS-PAGE suggested that purified collagen from S. japonicus was a 1 alpha trimer (about 135 kDa) while 1 alpha chain resembling alpha(1) chain of type I collagen of vertebrate. The thermal stability temperature (T-s) was 57.0 degrees C as measured by DSC, about 5.0 degrees C lower than that of type I collagen of calf. Peptide mapping and amino acid analysis of PSC also revealed the difference between invertebrate and vertebrate. However, the presence of (alpha(1))(3) trimers was evident. (c) 2005 Elsevier Ltd. All rights reserved.