Title : Titration and exchange studies of liver fatty acid-binding protein with 13C-labeled long-chain fatty acids.

Pub. Date : 2002 Apr 30

PMID : 11969406






3 Functional Relationships(s)
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Protein Name
Organism
1 Uniformly (13)C-labeled long-chain fatty acids were used to probe ligand binding to rat liver fatty acid-binding protein (LFABP), an atypical member of the fatty acid-binding protein (FABP) family that binds more than one molecule of long-chain fatty acid, accommodates a variety of diverse ligands, and exhibits diffusion-mediated lipid transport to membranes. Fatty Acids fatty acid binding protein 1 Rattus norvegicus
2 Two sets of (1)H-(13)C resonances were found in a titration series of NMR spectra for oleate-LFABP complexes, indicating that two molecules of the fatty acid are situated in the protein cavity. Fatty Acids fatty acid binding protein 1 Rattus norvegicus
3 In light of these NMR measurements, possible molecular mechanisms for the ligand-exchange process are evaluated and implications for the anomalous fatty acid transport mechanism of LFABP are discussed. Fatty Acids fatty acid binding protein 1 Rattus norvegicus