Soliternova I B, Nikul'cheva N G, Eliseeva L A
Ukr Biokhim Zh (1978). 1988 Sep-Oct;60(5):14-9.
Unlike the rabbit blood plasma the high-activity triglyceride lipase which does not require a protein cofactor and is resistant to 1 M of NaCl has been revealed in the liver of this animal. Rapid freezing of the liver tissue by liquid nitrogen before homogenization induced a sharp increase in the enzyme activity level and extraction of the active enzyme without heparin usually added to the homogenate. The specific activity of hepatic lipase purified from the ordinary heparin-containing homogenate by affinity chromatography on heparin-sepharose 4B was equal to 3800 microM of FFA/h per mg of protein. If the homogenate previously treated with liquid nitrogen was used as a source of enzyme, the specific activity of hepatic lipase was higher, namely, 13,000 and 19,000 microM of FFA/h per mg of protein in the presence or absence of heparin, respectively.
与兔血浆不同，在这种动物的肝脏中发现了一种高活性甘油三酯脂肪酶，它不需要蛋白质辅因子，并且对1M的NaCl具有抗性。在匀浆前用液氮快速冷冻肝脏组织会导致酶活性水平急剧增加，并且在通常不添加到匀浆中的肝素的情况下也能提取到活性酶。通过肝素琼脂糖4B亲和层析从普通含肝素匀浆中纯化的肝脂肪酶的比活性等于每毫克蛋白质3800微摩尔FFA/小时。如果将先前用液氮处理过的匀浆用作酶源，肝脂肪酶的比活性更高，即在有或没有肝素的情况下，分别为每毫克蛋白质13000和19000微摩尔FFA/小时。
