Surface potential of phosphatidylserine monolayers. II. Divalent and monovalent ion binding.
Ion binding constants for phosphatidylserine membranes have been derived from the variation of the surface potential of phosphatidylserine monolayers with divalent cation concentrations in the presence of various monovalent salts in the aqueous subphase. The observed surface potential data for the monolayers, analyzed by use of the Gouy-Chapman diffuse potential theory, together with a simple binding reaction formula, yield, for Ca2+, Mg2+, Na+ and (Me)4N+ binding constant values of 30 M-1, 10 M-1, 0.6 M-1 and 0.05 M-1, respectively. The effect of pH on surface potential of phosphatidylserine monolayers was found to be dependent upon ionic species other than H+ in the subphase solution. The distinction between apparent and intrinsic dissociation constants of H+ for biomolecules was made in terms of ion binding due to other ions at the same site as for H+ in biomolecules.
D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D002413:Cations, Divalent / Q000378:metabolism*; D002414:Cations, Monovalent / Q000378:metabolism*; D002417:Cattle; D008563:Membrane Lipids / Q000378:metabolism*; D008564:Membrane Potentials; D010718:Phosphatidylserines / Q000378:metabolism*; D012492:Salts; D013499:Surface Properties
D002413:Cations, Divalent; D002414:Cations, Monovalent; D008563:Membrane Lipids; D010718:Phosphatidylserines; D012492:Salts