Glycosylation of endothelial lipase at asparagine-116 reduces activity and the hydrolysis of native lipoproteins in vitro and in vivo

We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL. The current study demonstrates that mutag...

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Autors principals:	Robert J. Brown, Gwen C. Miller, Griffon Nathalie, Christopher J. Long, Daniel J. Rader
Format:	Artigo
Idioma:	Inglês
Publicat:	Elsevier 2007-05-01
Col·lecció:	Journal of Lipid Research
Matèries:	lipase lipoprotein hydrolysis adenovirus glycosylation site-directed mutagenesis heparin
Accés en línia:	http://www.sciencedirect.com/science/article/pii/S002222752043559X
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