Abstract
A number of reactive dichlorotriazine dyes specifically and irreversibly inactivate pig heart lactate dehydrogenase, yeast glucose 6-phosphate dehydrogenase and yeast hexokinase at sites competitive with NAD+, NADP+, and ATP respectively. Monochlorotriazine dyes, including Cibacron Blue F3G-A, do not inactivate lactate dehydrogenase but display high affinity and thus inhibit the inactivation by dichlorotriazine dyes. These data are interpreted in terms of the ability of nucleotide-binding enzymes to bind polysulphonated aromatic chromophores.