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Substrate specificity of rat sera IgG antibodies with peroxidase and oxidoreductase activities
Author(s) -
Ikhmyangan Erdenechimeg N.,
Vasilenko Nataliya L.,
Sinitsina Ol'ga I.,
Buneva Valenti.,
Nevinsky Georgy A.
Publication year - 2006
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.787
Subject(s) - peroxidase , chemistry , horseradish peroxidase , oxidoreductase , polyclonal antibodies , biochemistry , substrate (aquarium) , oxidizing agent , enzyme , antibody , biology , organic chemistry , immunology , ecology
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, α‐naphthol, and NADH but, in contrast to HRP, cannot oxidize adrenalin. In contrast to IgGs, HRP cannot oxidize phenol, p ‐dihydroquinone, or α‐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. Copyright © 2006 John Wiley & Sons, Ltd.