AI Article Synopsis
- A detailed procedure for isolating glutamate dehydrogenase (GDH) from human liver is outlined, using ion-exchange and affinity chromatography techniques.
- The voltammetric behavior of human and bovine GDH, along with rabbit anti-human GDH antibody, was optimized, achieving lower detection limits of 0.2 mg l-1 for human GDH and 1.2 mg l-1 for bovine GDH.
- The study also investigated the interaction between human GDH and rabbit anti-human GDH antibody using the optimized voltammetric method.
Article 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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| http://dx.doi.org/10.1039/an9901500617 | DOI Listing |
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