Effect of anions on the structure of glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle

Glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle undergoes reversible partial dissociation into 4.2–4.5 S fragments at +4°C and at protein concentrations as high as 8–9 mg/ml, depending upon the anion species present. The order of effectiveness of various anions in dissociating activity corresponds to their position in the Hofmeister series: bromide > nitrate > chloride > acetate > sulfate > phosphate=citrate. Quite similar is the order of activity of anions in their influence on the thermal stability of the dehydrogenase.