Strohfeldt P, Heugel C
Biochem Biophys Res Commun. 1984 May 31;121(1):87-94. doi: 10.1016/0006-291x(84)90691-0.
Triglyceride lipase activity was determined in particulate and soluble fractions from rat skeletal muscle homogenates. The fractions exhibited an acid (pH 5,0) optimum with an impressive enhancement in the combined P17 /100 fraction. Methylamine inhibited this acid lipase activity. A further lipase was observed with maximal activity at pH 7,0 and only a small enhancement in the combined P17 /100 fraction and inhibition by diethyl p-nitrophenyl-phosphate but not by protamine sulfate. Lipoprotein lipase activity was identified by the following in vitro criteria: Stimulation of activity by serum, maximal activity at alkaline pH (pH 8,5 - 9,0) and inhibition of activity by NaCl and protamine sulfate. There was a definite enhancement of lipoprotein lipase activity in the combined P17 /100 fraction after the lipase activity has been washed out from the capillary bed with heparin.
测定了大鼠骨骼肌匀浆颗粒部分和可溶部分中的甘油三酯脂肪酶活性。这些部分在pH 5.0时表现出最适酸性，在合并的P17/100部分中有显著增强。甲胺抑制这种酸性脂肪酶活性。还观察到另一种脂肪酶，其在pH 7.0时活性最高，在合并的P17/100部分中仅有少量增强，且被对硝基苯磷酸二乙酯抑制，但不被硫酸鱼精蛋白抑制。脂蛋白脂肪酶活性通过以下体外标准来鉴定：血清刺激活性、在碱性pH（pH 8.5 - 9.0）时活性最高以及被氯化钠和硫酸鱼精蛋白抑制活性。在用肝素从毛细血管床洗脱出脂肪酶活性后，合并的P17/100部分中的脂蛋白脂肪酶活性有明显增强。
