Substrate specificity of rat sera IgG antibodies with peroxidase and oxidoreductase activities.
We have recently shown that intact IgGs from the sera of healthy Wistar rats oxidize 3,3'-diaminobenzidine (DAB) in the presence and in the absence of H(2)O(2) similar to horseradish peroxidase (HRP). Here we demonstrate for the first time that the peroxidase and oxidoreductase activities of IgGs can efficiently oxidize not only DAB but also o-phenylendiamine, phenol, p-dihydroquinone, alpha-naphthol, and NADH but, in contrast to HRP, cannot oxidize adrenalin. In contrast to IgGs, HRP cannot oxidize phenol, p-dihydroquinone, or alpha-naphthol in the absence of H(2)O(2). In contrast to plant and mammalian peroxidases, IgGs were more universal in their metal dependence. The specific wide repertoire of polyclonal peroxidase and oxidoreductase IgGs oxidizing various substances could play an important role in protecting the organism from oxidative stress and serve as an additional natural system destroying different toxic, carcinogenic, and mutagenic compounds.
Ikhmyangan
Erdenechimeg N
EN
Institute of Cytology and Genetics, Siberian Division of Russian Academy of Sciences, 10 Lavrentieva Avenue, Novosibirsk, Russia.
Vasilenko
Nataliya L
NL
Sinitsina
Ol'ga I
OI
Buneva
Valentina N
VN
Nevinsky
Georgy A
GA
D000818:Animals; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D006735:Horseradish Peroxidase / Q000097:blood / Q000378:metabolism*; D007074:Immunoglobulin G / Q000097:blood* / Q000378:metabolism*; D007700:Kinetics; D008670:Metals / Q000378:metabolism; D009284:Naphthols / Q000378:metabolism; D010084:Oxidation-Reduction; D019800:Phenol / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity
D007074:Immunoglobulin G; D008670:Metals; D009284:Naphthols; D019800:Phenol; D006735:Horseradish Peroxidase