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Characterization of cDNA encoding the mouse hepatic triglyceride lipase and expression by in vitro translation
Author(s) -
Chang Shau-Feng,
Netter Hans Jürgen,
Will Hans
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80910-u
Subject(s) - complementary dna , hepatic lipase , triglyceride lipase , biochemistry , open reading frame , microbiology and biotechnology , cdna library , lipoprotein lipase , biology , lipase , nucleic acid sequence , translation (biology) , peptide sequence , messenger rna , gene , chemistry , enzyme
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.