Studies on the anion binding selectivity of sarcoplasmic reticulum membranes by 35Cl-NMR.
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 greater than phosphate greater than sulfate much greater than iodide greater than oxalate greater than bromide greater than chloride much greater than 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.
Vetter
I R
IR
Institut für Biophysikalische Chemie und Biochemie, Johann-Wolfgang-Goethe-Universität, Frankfurt am Main, F.R.G.
Hanssum
H
H
Bäumert
H G
HG
D001665:Binding Sites; D001965:Bromides; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D002712:Chlorides / Q000378:metabolism*; D005459:Fluorides; D009682:Magnetic Resonance Spectroscopy; D010070:Oxalates; D019815:Oxalic Acid; D010710:Phosphates; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives; D012519:Sarcoplasmic Reticulum / Q000737:chemistry*; D013431:Sulfates; D014638:Vanadates
D001965:Bromides; D002712:Chlorides; D010070:Oxalates; D010710:Phosphates; D013431:Sulfates; C057654:pyridoxal phosphate-6-azophenyl-2'-sulfonic acid; D014638:Vanadates; D011732:Pyridoxal Phosphate; D019815:Oxalic Acid; D005459:Fluorides