Summary An o‐diphenol: oxygen oxidoreductase (E.C. 1.10.3.1) has been purified from potato tubers. The enzyme shows a similar affinity for a range of substrates although the affinity is highest for chlorogenic acid, which occurs naturally in potato tubers. The affinity for oxygen is relatively low (Km= 2.23 × 10−4 m). The pattern of activity over a range of pH values varied considerably with different substrates. Ultracentrifuge studies and agar gel electrophoresis suggest the preparation is relatively pure although throughout purification the preparation showed an increasing cresolase as well as o‐diphenoloxidase activity. It is suggested that the cresolase activity is a normal component of the enzyme activity which may well be of importance in vivo. The high potency of a number of inhibitors including the copper‐specific 3:4 dichlorophenyl serine suggests that this metal is an integral part of the prosthetic group.
No takes yet. Share an insight, caveat, or question.
Abukharma et al. (1966) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: