Abstract
Anion binding sites on the membranes of sarcoplasmic reticulum vesicles can be characterized with the aid of 35Cl-NMR. Titration experiments with a series of different anions reveal that multivalent, phosphate-like anions bind much stronger to SR vesicles than monovalent anions like halides whereas oxalate seems to have an intermediate position. The binding strength decreases with decreasing ionic radius according to the following sequence: vanadate > phosphate>sulfate ≫ iodide > oxalate > bromide > chloride > fluoride. This is also reflected by increasing dissociation constants. Although vanadate in absolute terms replaces much more chloride than either, phosphate or sulfate, their dissociation constants are very similar. This implicates a special binding mechanism for vanadate. Phosphate analoguous compounds like pyridoxalphosphate-6-azophenyl-2′-sulfonic acid and its 4′-nitroderivative show the strongest binding.
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