Article
Characterization of recombinant wild type and site-directed mutations of apolipoprotein C-III: lipid binding, displacement of ApoE, and inhibition of lipoprotein lipase.
Biochemistry - 8 Aug 2000
Liu H, Talmud P J, Lins L, Brasseur R, Olivecrona G, Peelman F, Vandekerckhove J, Rosseneu M, Labeur C
Abstract excerpt
The physicochemical properties of recombinant wild type and three site-directed mutants of apolipoprotein C-III (apoC-III), designed by molecular modeling to alter specific amino acid residues implicated in lipid binding (L9T/T20L, F64A/W65A) or LPL inhibition (K21A), were compared. Relative lipid binding efficiencies to dimyristoylphosphatidylcholine (DMPC) were L9T/T20L > WT >K21A > F64A/W65A with an inverse...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.