title: Neutral proteinases in muscle tissue and cells.
abstract: Chymase isolated from rat skeletal muscle tissue was compared with other proteinases in rat muscle that hydrolyse chymase substrates. These enzymes were purified from the 100,000 x g supernatant of hind limb rat muscles homogenized with 0.15 M NaCl-20 mM phosphate buffer, pH 7.2. A metallproteinase (MMP-7-ase) and a serine proteinase (ATN-ase) were partially characterized, and shown to be different from chymase.
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D053818:Chymases; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008666:Metalloendopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D051381:Rats; D012697:Serine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D012697:Serine Endopeptidases; D053818:Chymases; D008666:Metalloendopeptidases