Chang S F, Netter H J, Will H
Max-Planck-Institut für Biochemie, Martinsried, Germany.
FEBS Lett. 1991 Sep 2;289(1):69-72. doi: 10.1016/0014-5793(91)80910-u.
A cDNA coding for the mouse hepatic triglyceride lipase has been isolated from a mouse liver cDNA library. The nucleotide sequence of the cDNA shows an open reading frame encoding a polypeptide of 510 amino acids that is 91.5% and 86% homologous to rat and human hepatic lipase, respectively. The most drastic protein sequence divergence is found at the carboxyterminal end which was speculated to harbour one heparin-binding site. By in vitro translation of cRNA in the presence of pancreatic membranes the hepatic lipase was shown to be glycosylated and to have an electrophoretic mobility of 53 kDa.
从小鼠肝脏cDNA文库中分离出了编码小鼠肝脏甘油三酯脂肪酶的cDNA。该cDNA的核苷酸序列显示一个开放阅读框,编码一个由510个氨基酸组成的多肽,该多肽与大鼠和人肝脏脂肪酶的同源性分别为91.5%和86%。在推测含有一个肝素结合位点的羧基末端发现了最显著的蛋白质序列差异。通过在胰腺膜存在的情况下对cRNA进行体外翻译,结果显示肝脏脂肪酶被糖基化,电泳迁移率为53 kDa。