PEROXIDATIC ACTIVITY OF METALLOPORPHYRIN BINDING TO SERUM-ALBUMIN - ENHANCEMENT EFFECT OF SERUM-ALBUMIN ON METALLOPORPHYRIN CATALYZED LUMINOL CHEMILUMINESCENCE REACTION

The metalloporphyrin (M-P) catalyzed luminol-H2O2 chemiluminescence (C L) system can be significantly enhanced in the presence of serum album ins. The enhancement may be explained in terms of the formation of a m olecular complex between MP and serum albumin. The hydrophobic and coo rdination interactions between M-P and serum albumin were confirmed by comparing the degree of enhancement by the protein on different types of M-P catalyzed CL reactions and by comparing the catalytic activity of M-P/bovine serum albumin (BSA) and M-P/BSA/anti-BSA complexes. Onl y the non-ionic M-P catalyzed CL reaction was significantly enhanced, and the enhanced CL reaction was inhibited by an immunoreaction. The o ptimum conditions of the M-P/albumin complex catalyzed CL reaction wer e evaluated by using a flow-injection system, which was very similar t o that using hemoglobin as the catalyst. A brief prospective on the ge neral applicability of the enhanced CL reaction for the determination of serum albumin (2.5-500 mu g/ml) is given.