Purification of an endogenous 68,000-dalton inhibitor of Ca2+-activated neutral protease from chicken skeletal muscle.
An endogenous inhibitor of Ca2+-activated neutral protease has been purified from chicken skeletal muscle. The inhibitor, which was isolated by acid treatment and four subsequent chromatographic procedures, is a protein composed of a single polypeptide having a molecular weight of 68,000. It contains large amounts of glycine, proline and glutamic acid but the contents of aromatic amino acids are low. The inhibitor appeared to act on Ca2+-activated neutral protease in a stoichiometric manner, suggesting a complex formation. The inhibitory action was not caused by sequestering of Ca2+. The inhibitor did not inhibit other well-known thiol proteases, but was slightly effective for trypsin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002645:Chickens; D002845:Chromatography; D010450:Endopeptidases / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D011480:Protease Inhibitors / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D011480:Protease Inhibitors; D010450:Endopeptidases; D002118:Calcium