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.
D000249:Adenosine Monophosphate / Q000378:metabolism*; D000818:Animals; D001051:Apoenzymes / Q000378:metabolism*; D001059:Apoproteins / Q000378:metabolism*; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D001667:Binding, Competitive; D003600:Cytosol / Q000201:enzymology*; D003956:Dialysis; D009206:Myocardium / Q000201:enzymology; D011732:Pyridoxal Phosphate / Q000378:metabolism; D013053:Spectrophotometry; D013552:Swine
D001051:Apoenzymes; D001059:Apoproteins; D000249:Adenosine Monophosphate; D011732:Pyridoxal Phosphate; D001219:Aspartate Aminotransferases