Author/Authors
Gabriela Alvite، نويسنده , , Santiago M. Di Pietro، نويسنده , , José A. Santomé، نويسنده , , Ricardo Ehrlich، نويسنده , , Adriana Esteves، نويسنده ,
DocumentNumber
1601814
Title Of Article
Binding properties of Echinococcus granulosus fatty acid binding protein
شماره ركورد
12358
Latin Abstract
EgFABP1 is a developmentally regulated intracellular fatty acid binding protein characterized in the larval stage of parasitic platyhelminth Echinococcus granulosus. It is structurally related to the heart group of fatty acid binding proteins (H-FABPs). Binding properties and ligand affinity of recombinant EgFABP1 were determined by fluorescence spectroscopy using cis- and trans-parinaric acid. Two binding sites for cis- and trans-parinaric acid were found (Kd(1) 24±4 nM, Kd(2) 510±60 nM for cis-parinaric acid and Kd(1) 32±4 nM, Kd(2) 364±75 nM for trans-parinaric). A putative third site for both fatty acids is discussed. Binding preferences were determined using displacement assays. Arachidonic and oleic acids presented the highest displacement percentages for EgFABP1. The Echinococcus FABP is the unique member of the H-FABP group able to bind two long chain fatty acid molecules with high affinity. Structure–function relationships and putative roles for EgFABP1 in E. granulosus metabolism are discussed.
From Page
293
NaturalLanguageKeyword
Echinococcus granulosus , EgFABP1 , Binding property , Fatty acid , Fatty acid binding protein
JournalTitle
Studia Iranica
To Page
302
To Page
302
Link To Document