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

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D. S. Jairajpuri¹, S. Fatima¹, and M. Saleemuddin^1,2*

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

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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.

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KEY WORDS: antigen-antibody complex, anti-glycation agents, F(ab)'₂, F(ab)', glycation

DOI: 10.1134/S0006297908110102

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