Characterization of cDNA encoding the mouse hepatic triglyceride lipase and expression by in vitro translation.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Chang SF,Netter HJ,Will H

doi

10.1016/0014-5793(91)80910-u

subject

Has Abstract

pub_date

1991-09-02 00:00:00

pages

69-72

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80910-U

journal_volume

289

pub_type

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