[Co-oxidation of phenols and 4-aminoantipyrene catalyzed by microperoxidase and their complexes with proteins].
The kinetic parameters of 4-aminoantipyrine (AAP) co-oxidation with phenol or p-iodophenol in a wide range of hydrogen peroxide concentrations were compared for microperoxidases MP-8, MP-9, MP-11, horseradish peroxidase (HRP) and peroxidase of Arthromyces ramosus (PAR). The peroxidatic activity increased in the following order: HRP > PAR > MP-9 > MP-8 > MP-11. Microperoxidase complexes with human serum albumin (1:1) retained their peroxidatic activity at high H2O2 concentrations, protecting haem from destruction by active radicals. Monoclonal antibodies against porphyrin decreased the peroxidatic activities of three microperoxidases during co-oxidation of AAP and phenol and protected haem. Inert proteins (BSA, ovalbumin) had little effect on the HRP activity, whereas enzyme-specific antibodies strongly activated HRP at high concentrations of hydrogen peroxide, thereby forming an immune complex protecting HRP from its dissociation down to haem and the apoenzyme.
Metelitsa
D I
DI
Arapova
G S
GS
Vidzhinaĭte
R A
RA
Demcheva
M V
MV
Litvinchuk
A V
AV
Razumas
V I
VI
D000595:Amino Acid Sequence; D000675:Ampyrone / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D005658:Fungi / Q000201:enzymology; D007700:Kinetics; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D010636:Phenols; D011506:Proteins; D000675:Ampyrone; D010544:Peroxidases; C021799:microperoxidase
Sopriazhennoe okislenie fenolov i 4-aminoantipirina, kataliziruemoe mikroperoksidazami i ikh kompleksami s belkami.