Nikul'cheva N G, Soliternova I B, Eliseeva L A
Biokhimiia. 1990 Jan;55(1):173-80.
Using affinity chromatography on heparin-Sepharose 4B, triglyceride lipase was isolated from rabbit liver tissue and purified. The specific activity of the enzyme isolated from the usual homogenate was equal to (3.8 +/- 1.2) x 10(3) mumol/hour/mg protein. After treatment of liver tissue homogenates with liquid nitrogen the enzyme activity increased severalfold as compared to the enzyme isolated from the usual homogenate. The dependences of the triglyceride lipase activity on the concentrations of the protein (enzyme), substrate (triglyceride), albumin (fatty acid acceptor) and pH were studied. The isolated form of liver triglyceride lipase was found to have two pH optima at 6.5 and 8.5.
通过肝素-琼脂糖4B亲和层析，从兔肝组织中分离并纯化了甘油三酯脂肪酶。从常规匀浆中分离得到的酶的比活性为(3.8±1.2)×10³微摩尔/小时/毫克蛋白质。用液氮处理肝组织匀浆后，与从常规匀浆中分离得到的酶相比，酶活性提高了几倍。研究了甘油三酯脂肪酶活性对蛋白质（酶）、底物（甘油三酯）、白蛋白（脂肪酸受体）浓度和pH的依赖性。发现分离得到的肝甘油三酯脂肪酶在pH 6.5和8.5时有两个最适pH值。
