Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.:I. Purification and Characterization
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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: 1.8mM) or strontium (optimum concentration: 10mM) ions. The protease was inhibited by leupeptin, which is known to be a strong inhibitor of papain, cathepsin B, trypsin, and plasmin.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
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