Abstract
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.
