Effect of pH, ionic strength and univalent inorganic ions on the reconstitution of aspartate aminotransferase

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Abstract
1. The effect of pH change on the reconstitution of aspartate aminotransferase (EC 2.6.1.1), i.e. the reactivation of the apoenzyme with coenzyme (pyridoxal phosphate and pyridoxamine phosphate), was studied in the pH range 4.2–8.9 by using three buffer systems at concentrations ranging from 0.025 to 0.1m. 2. Although the profile of the reconstitution rate–pH curve in the range pH5.2–6.8 (covered by sodium cacodylate–HCl buffer) reflects the influence of the H+ concentration on the reconstitution process, the profile of the curve in the pH ranges 4.2–5.6 and 7.2–8.25 (covered respectively by sodium acetate–acetic acid and Tris–HCl buffers) appears to be influenced by the ionic strength of the buffer. 3. The reconstitution is also influenced by univalent inorganic ions such as halide ions and, to a lesser extent, alkali metal ions, which are known to alter the water structure.