ORBi: Poncin Jacques - Cloning and structure analysis of the rat apolipoprotein A-I cDNA

Reference : Cloning and structure analysis of the rat apolipoprotein A-I cDNA


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/26668

Title :	Cloning and structure analysis of the rat apolipoprotein A-I cDNA
Language :	English
Author, co-author :	Poncin, Jacques [ > > ]
	Martial, Joseph [Université de Liège - ULg > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
	Gielen, Jacques [ > > ]
Publication date :	1984
Journal title :	European Journal of Biochemistry
Publisher :	Blackwell Science
Volume :	140
Issue/season :	3
Pages :	493-8
ISSN :	0014-2956
e-ISSN :	1432-1033
City :	Oxford
Country :	United Kingdom
Keywords :	[en] Animals ; Apolipoprotein A-I ; Apolipoproteins/genetics ; Base Composition ; Base Sequence ; Cell-Free System ; Chemical Phenomena ; Chemistry ; Cloning, Molecular ; Codon ; *Dna ; Humans ; Immunochemistry ; Male ; RNA, Messenger/isolation & purification ; Rabbits ; Rats ; Rats, Inbred Strains
Abstract :	[en] 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 lipid/protein binding or lecithin-cholesterol acyltransferase activation.
Permalink :	http://hdl.handle.net/2268/26668
DOI :	10.1111/j.1432-1033.1984.tb08129.x
Other URL :	http://www3.interscience.wiley.com/journal/120761521/abstract?CRETRY=1&SRETRY=0
Mentions required by the publisher for OA :	1984/05/02

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