Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase.
Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase.
复制标题
牛胰腺胆固醇酯酶/溶血磷脂酶的克隆。
DOI：
10.1016/0006-291x(89)91811-1
复制
发表时间：
1989
影响因子：
3.1
通讯作者：
Lange,LG
中科院分区：
文献类型：
--
作者：
Kyger,EM;Wiegand,RC;Lange,LG
编码牛胰腺胆固醇酯酶的cDNA克隆已被测序。胰腺胆固醇酯酶将膳食胆固醇酯水解为胆固醇和游离脂肪酸，然后从肠道吸收。北方印迹显示，在牛胰腺中1.9磷酸酶处的阳性信号比小牛胰腺中的强得多，表明该酶的诱导是由于mRNA的转录增加或稳定性。这种酶的一级结构与大鼠胰腺溶血磷脂酶的一级结构相似。我们发现，同质的人和牛胰腺胆固醇酯酶具有高水平的溶血磷脂酶活性，表明这两种活性存在于同一蛋白质中。因此，膳食中性脂质和极性脂质的代谢可能通过单一酶联系起来。
A cDNA clone encoding for the bovine pancreatic cholesterol esterase has been sequenced. Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. Therefore, the metabolism of dietary neutral lipids and polar lipids may be linked through a single enzyme.