BIOMIMIC OF PEROXIDASE AND ENZYMATIC ASSAY FOR ASCORBIC-ACID

Mn-T(4-TAP)P rakis(4-trimethylammoniumphenyl)-21H,23H-porphine] has be en synthesized and used to mimic the active group of horseradish perox idase. The catalytic behavior of the mimetic enzyme with ascorbic acid as its substrate has been studied, and accurate determination of 0.1- 10.0 mu g/ml ascorbic acid achieved. The method is simple, rapid and h ighly selective. No interference by other biological substances contai ned in body fluids was found. The effectiveness of this mimetic enzyme was compared with four other mimics (Mo-TPPS4, and its Fe and Mn anal ogs, Cu-TC(4-TAP)P and horseradish peroxidase itself) and found to be the most effective mimic.