Sternby B
Dept. of Medical and Physiological Chemistry, University of Lund, Sweden.
Scand J Gastroenterol. 1993 Apr;28(4):347-51. doi: 10.3109/00365529309090254.
A pure lipase has been isolated from extracts of the human pancreas. The purification process includes centrifugation, two ion-exchange chromatography steps, and one gel filtration step. Compared with other reports, a high recovery, large amounts, and a high specific activity were obtained. Lipase is present at 1-2 mg/g in the pancreatic gland. In the absence of colipase and bile salts with tributyrine as substrate, the specific activity at room temperature and at pH 7.0 is 4000 mumol/min/mg. It increases to 8000-10,000 in the presence of colipase and bile salts at a temperature of 37 degrees C. The fate of the other human lipolytic proteins during the different purification steps is also indicated. Lipase purified by this method has been used for crystallization.
已从人胰腺提取物中分离出一种纯脂肪酶。纯化过程包括离心、两步离子交换色谱步骤和一步凝胶过滤步骤。与其他报道相比，获得了高回收率、大量且高比活性的脂肪酶。脂肪酶在胰腺中的含量为1 - 2毫克/克。以三丁酸甘油酯为底物，在没有辅脂酶和胆盐的情况下，室温及pH 7.0时的比活性为4000微摩尔/分钟/毫克。在37摄氏度下存在辅脂酶和胆盐时，比活性会增加到8000 - 10000。还指出了其他人体脂解蛋白在不同纯化步骤中的去向。用这种方法纯化的脂肪酶已用于结晶。
