Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.
Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.
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来自鸡骨骼肌的钙激活中性蛋白酶的研究。
DOI：
10.1093/oxfordjournals.jbchem.a132111
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发表时间：
1978
影响因子：
2.7
通讯作者：
K. Imahori
中科院分区：
文献类型：
--
作者：
S. Ishiura;H. Murofushi;K. Suzuki;K. Imahori
从鸡骨骼肌粗提物中纯化了2,700倍的钙激活中性蛋白酶。纯化的蛋白酶在有或没有SDS的聚丙烯酰胺凝胶电泳上迁移为单一条带。其分子量为80，000，最适活性pH为7.7。该活性严格要求钙（最佳浓度：1.8mM）或锶（最佳浓度：10 mM）离子的存在。蛋白酶被亮抑酶肽抑制，亮抑酶肽已知是木瓜蛋白酶、组织蛋白酶B、胰蛋白酶和纤溶酶的强抑制剂。
A calcium-activated neutral protease was purified 2,700-fold over the crude extract from chicken skeletal muscle. The purified protease migrated as a single band on polyacrylamide gel electrophoresis with or without SDS. Its molecular weight was 80,000 and pH optimum for activity was 7.7. The activity required strictly the presence of calcium (optimum concentration: 1.8 mM) or strontium (optimum concentration: 10 mM) ions. The protease was inhibited by leupeptin, which is known to be a strong inhibitor of papain, cathepsin B, trypsin, and plasmin.