Chloride-37 nuclear magnetic resonance spectroscopic study of binding of salicylic acid and other hydroxybenzoic acids to the band 3 anion transport protein of human erythrocytes.
Chloride-37 nuclear magnetic resonance spectroscopy was used to investigate the displacement of chloride (Cl-) from binding sites on band 3 anion transport protein in human erythrocytes by salicylic acid and five other hydroxybenzoic acids (HAs). All the HAs studied displaced Cl- from these binding sites. The association constants for binding of the HAs to band 3 anion transport protein were larger than that for Cl- and dependent on the specific structural features of the molecule, rather than general physicochemical characteristics.
Minami
T
T
Department of Pharmacy, University of Sydney, New South Wales, Australia.
Price
W S
WS
Cutler
D J
DJ
D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D027321:Anion Transport Proteins; D001665:Binding Sites; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D002712:Chlorides / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D062385:Hydroxybenzoates / Q000378:metabolism*; D007554:Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D012459:Salicylates / Q000378:metabolism*; D020156:Salicylic Acid; D013057:Spectrum Analysis / Q000379:methods
D001457:Anion Exchange Protein 1, Erythrocyte; D027321:Anion Transport Proteins; D002352:Carrier Proteins; D002712:Chlorides; D062385:Hydroxybenzoates; D007554:Isotopes; D012459:Salicylates; D020156:Salicylic Acid