Open AccessCloning and structure analysis of the rat apolipoprotein A‐1 cDNA
Author(s) -
PONCIN Jacques E.,
MARTIAL Joseph A.,
GIELEN Jacques E.
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08129.x
Subject(s) - complementary dna , apolipoprotein b , biology , biochemistry , microbiology and biotechnology , apolipoprotein e , acyltransferase , lipoprotein , polysome , peptide sequence , cholesterol , gene , rna , ribosome , medicine , disease , pathology
Apolipoprotein A‐I, the major protein in mammalian high‐density lipoprotein, acts as a cofactor for lecithin‐cholesterol acyltransferase during the formation of cholesterol ester and as such, is thought to promote cholesterol efflux from peripheral cells to the liver. In this paper, we report the partial purification of rat liver apolipoprotein A‐I mRNA by a polysome immunoadsorption technique, and its cDNA cloning. Isolation of two overlapping cDNA clones enabled us to derive the whole rat apolipoprotein A‐I cDNA coding sequence. Comparison of the deduced protein sequence with its human counterpart reveals a striking homology between the prepropeptide precursors. Both mature protein amino‐terminal regions are very homologous, suggesting that this particular domain could be involved in liquid/protein binding or lecithin‐cholesterol acyltransferase activation.