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Polyclonal antibodies inhibit the glycation‐induced inactivation of bovine Cu,Zn‐superoxide dismutase
Author(s) -
Jabeen Rukhsana,
Saleemuddin M.
Publication year - 2006
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20040201
Subject(s) - superoxide dismutase , polyclonal antibodies , chemistry , incubation , biochemistry , enzyme , fructose , glycation , dismutase , antibody , ribose , microbiology and biotechnology , biology , immunology , receptor
In vitro incubation of bovine Cu,Zn‐SOD (Cu,Zn‐superoxide dismutase) with glucose, ribose or fructose results in a remarkable inactivation of the enzyme. There was a progressive decrease in enzyme activity on incubation with glucose and, at the end of 7 days, only 26% of the initial activity remained. The inactivation was accompanied by a parallel decrease in the amount of protein detectable on gels after SDS/PAGE. Reaction of the sugars with SOD was ascertained using an immunoblot assay in which sugar‐incubated SOD was derivatized with 2,4‐dinitrophenylhydrazine and allowed to react with the dinitrophenol‐specific antibody. Affinity purified antibodies from the sera of rabbits immunized with bovine SOD were highly effective in restricting the inactivation of the enzyme induced by glucose, ribose or fructose.