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 x 10(-6) M-1 and 31.4 x 10(-6) M-1, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.