Purification and properties of a novel latent proteinase showing myosin heavy chain-degrading activity from threadfin-bream muscle.
Purification and properties of a novel latent proteinase showing myosin heavy chain-degrading activity from threadfin-bream muscle.
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一种新型潜在蛋白酶的纯化和特性，显示来自鳊鱼肌肉的肌球蛋白重链降解活性。
DOI：
10.1093/oxfordjournals.jbchem.a123090
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发表时间：
1990
影响因子：
2.7
通讯作者：
Y. Shimizu
中科院分区：
文献类型：
--
作者：
M. Kinoshita;H. Toyohara;Y. Shimizu
通过结合 DEAE-纤维素、Con A-Sepharose、Arg-Sepharose 和 Shim-pack HAC 色谱法，从鲂鱼肌肉中纯化出一种新型潜在蛋白酶，其活性通过在 NaCl 存在下加热来诱导。该蛋白酶是具有单体亚基结构的糖蛋白；根据 SDS-PAGE 分析，Mr 估计为 77,000。在 pH 7.0 和 60 摄氏度、2-4% NaCl 存在的情况下，蛋白酶可水解 Boc-Leu-Thr-Arg-MCA 以及肌球蛋白重链。根据大豆胰蛋白酶抑制剂、亮肽素和抗痛作用，将蛋白酶分类为丝氨酸蛋白酶。
A novel latent proteinase of which activity was induced by heating in the presence of NaCl was purified to homogeneity from threadfin-bream muscle by a combination of DEAE-cellulose, Con A-Sepharose, Arg-Sepharose, and Shim-pack HAC chromatographies. This proteinase was a glycoprotein having a monomeric subunit structure; Mr was estimated to be 77,000 on SDS-PAGE analysis. The proteinase hydrolyzed Boc-Leu-Thr-Arg-MCA as well as myosin heavy chain in the presence of 2-4% NaCl at pH 7.0 and at 60 degrees C, optimally. The proteinase was classified as serine proteinase based on the effects of soybean trypsin inhibitor, leupeptin, and antipain.