Sohár I, Fekete E, Yorke G, Roisen F, Bird J W
Rutgers University Anatomy Department, UMDNJ-Rutgers Medical School Piscataway 08854.
Biomed Biochim Acta. 1987;46(7):571-9.
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.
将从大鼠骨骼肌组织中分离出的糜酶与大鼠肌肉中其他水解糜酶底物的蛋白酶进行了比较。这些酶是从用0.15 M NaCl - 20 mM磷酸盐缓冲液（pH 7.2）匀浆的大鼠后肢肌肉的100,000 x g上清液中纯化得到的。对一种金属蛋白酶（MMP - 7酶）和一种丝氨酸蛋白酶（ATN酶）进行了部分特性鉴定，结果表明它们与糜酶不同。
