Rindler-Ludwig R, Patsch W, Sailer S, Braunsteiner H
Biochim Biophys Acta. 1977 Aug 24;488(2):294-304. doi: 10.1016/0005-2760(77)90187-4.
Hydrolysis of glycerol trioleate by human leucocytes was characterized and the enzymes responsible for this activity were obtained in a purified form by means of gel chromatography on Sephadex G-100 as well as by zonal ultracentrifugation followed by gel chromatography. The activity is localized in the granule fraction of leucocytes (15 000 X g, 20 min) and shows a sharp pH optimum at pH 5.25. As judged from the elution profile obtained by gel chromatography, two proteins are likely to contribute to the hydrolysis of glycerol trioleate. The approximate molecular weights of the two enzymes are 74 100 and 60 300, respectively. The activity is reduced in the presence of NaCl, KCl, CaCl2 as well as of p-hydroxymercuribenzoate. The enzymes are stable at -25 degrees C but loose about 50% of their activity within 48 h at 4 degrees C.
对人白细胞水解甘油三油酸酯的特性进行了研究，并通过在Sephadex G - 100上进行凝胶色谱以及区带超速离心后再进行凝胶色谱，以纯化形式获得了负责该活性的酶。该活性定位于白细胞的颗粒部分（15000×g，20分钟），在pH 5.25时显示出尖锐的最适pH值。从凝胶色谱获得的洗脱图谱判断，两种蛋白质可能有助于甘油三油酸酯的水解。这两种酶的近似分子量分别为74100和60300。在NaCl、KCl、CaCl2以及对羟基汞苯甲酸存在的情况下，活性会降低。这些酶在-25℃下稳定，但在4℃下48小时内会丧失约50%的活性。
