The dissociation constants of NAD-and NADP- dependent dehydrogenases for 2'-AMP and 5'-AMP were determined by affinity ele-trophoresis using 2'-AMP-and 5'-AMP-acrylamide copolymers. From the dissocation constants, it was found that NADP-dependent dehydrogenase (NADP-dependent DH) had a much stronger affinity to the immobilized 2'-AMP than did NAD-dependent dehydrogenase (NAD-dependent DH). On the other hand, NADP-dependent DH had a much weaker affinity to immobilized 5'-AMP than did NAD-dependent DH. The effects of NADP+ and NAD+ on the binding of NADP-dependent DH to the immobilized 2'-AMP or the binding of NAD-dependent DH to the immobilized 5'-AMP were also investigated by affinity electrpphoresis…