AFFINITY CHROMATOGRAPHY AND CONFORMATIONAL ISOMERS OF dCMP-AMINOHYDROLASE

Matrices containing ligands which interact with catalytic or allosteric sites have been successfuly used for the purification of the allosteric enzyme dCMP-aminohydrolase. This enzyme is eluted specifically by a competitive inhibitor from a matrix coated with ligands which interact with the catalytic sites of the enzyme. The allosteric activator elutes the enzyme from a matrix coated with hydrazide-UTP which behaves as an allosteric inhibitor exploiting the allosteric conformational changes of dCMP-aminohydrolase.