Neutral proteinases in muscle tissue and cells.
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.
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
D012697:Serine Endopeptidases; D053818:Chymases; D008666:Metalloendopeptidases