Abstract
Monoclonal antibodies to glucose oxidase (E.C. 1.1.3.4) from Aspergillus niger were prepared with apoenzyme as the antigen. Five of these antibodies, all of the IgG1 subisotype, were further characterized. They were affinity purified using an affinity column prepared by covalent immobilization of glucose oxidase via a spacer arm. Glucose oxidase lost its immunological reactivity with these monoclonal antibodies under direct covalent immobilization. The carbohydrate moiety of the enzyme is not immunogenic. None of the antibodies had any detectable effect on the catalytic properties of the enzyme. All the antibodies are directed towards segmental epitopes of the enzyme, and each enzyme subunit has more than one non-overlapping epitope. All five antibodies bound the non-native enzyme coated on ELISA plates in preference to the enzyme in solution.
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