Purification of rat uterine peroxidase

Using a combination of gel filtration, affinity chromatography on immobilized concanavalin A and hydrophobic adsorption chromatography, a peroxidase has been isolated from the uteri of oeastrogen-primed rats. The enzyme was purified some 306-fold with respect to the uterine extract and to greater than 95% homogeneity. The final product had an apparent molecular weight of 48 000, an absorption maximum at 412 nm (A412/A280 = 0.47) and a specific activity very similar to those of several other pure haemoprotein peroxidases.