Purification of human glutamate dehydrogenase (GDH) and an adsorptive voltammetric investigation of the interaction of GDH with rabbit anti-human GDH antibody |
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| Authors: | P Carty R O'Kennedy E Lorenzo Abad J M Fernández Alvarez J Rodriguez Flores M R Smyth K Tipton |
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| Affiliation: | School of Biological Sciences, Dublin City University, Ireland. |
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| Abstract: | A procedure for the isolation of glutamate dehydrogenase (GDH) from human liver, which involves the use of ion-exchange chromatography on diethylaminoethyl cellulose and affinity chromatography on guanosine triphosphate conjugated to Sepharose 4B, is described. The adsorptive voltammetric behaviour of human GDH, bovine GDH and rabbit anti-human GDH antibody was optimised with respect to accumulation potential, accumulation time and scan rate. The lower limits of detection were 0.2 and 1.2 mg l-1 for human and bovine GDH, respectively, and the lower limit of detection for rabbit anti-GDH antibody was 0.04 mg l-1. The interaction of human GDH with rabbit anti-human GDH antibody was also examined using this method. |
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