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Complexing of Glucose Oxidase with Anti-Glucose Oxidase Antibodies or the F(ab)'2/F(ab)' Fragments Derived Therefrom Protects Both the Enzyme and Antibody/Antibody Fragments against Glycation

D. S. Jairajpuri1, S. Fatima1, and M. Saleemuddin1,2*

1Department of Biochemistry, Aligarh Muslim University, Aligarh 202002, India

2Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India; fax: +915712721776; E-mail: msaleemuddin47@gmail.com

* To whom correspondence should be addressed.

Received January 28, 2008; Revision received March 27, 2008
Incubation of Aspergillus niger glucose oxidase with glucose, fructose, or ribose results in remarkable inactivation of the enzyme. Glucose oxidase incubated with the sugars migrated as a diffuse band of low intensity and silver stained poorly after SDS-PAGE. Purified anti-glucose oxidase antibodies and F(ab)'2 or F(ab)' derived therefrom were effective in restricting the inactivation of the enzyme induced by the sugars, providing up to 90% protection. The sugars also caused remarkable changes in the electrophoretic behavior of anti-glucose oxidase antibodies and the fragments, but complexing with glucose oxidase restricted the changes both in the enzyme and the antibody/antibody fragments.
KEY WORDS: antigen-antibody complex, anti-glycation agents, F(ab)'2, F(ab)', glycation

DOI: 10.1134/S0006297908110102