Interaction of AMP with cytosolic apo-aspartate aminotransferase

Interaction of cytosolic apo-aspartate aminotransferase with AMP has been studied under equilibrium conditions: e.g., equilibrium dialysis and spectrophotometric titration. Results show that a 1:1 stoichiometric complex AMP—apo-aspartate aminotransferase monomer is formed. The calculated dissociation constants with the two different experimental techniques are 40.4 × 10^?6 M^?1 and 31.4 × 10^?6 M^?1, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.