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Five monoclonal antibodies (mAbs) that recognize human glutamate dehydrogenase (GDH) have been selected and designated as monoclonal antibodies hGDH60-6, hGDH60-8, hGDH63-10, hGDH63-1, and hGDH91-14. A total of five mAbs recognizing differ-which inhibited human GDH activity. When total proteins of human homogenate separated by SDS- PAGE, were probed with mAbs, a single reactive protein band of 5 kDa, which co-migrated with purified recombinant human GDH was detected. When the purified GDH was incubated with each of the mAbs, its enzyme activity was inhibited by up to 58%. Epitope maping analysis identified, two subgroups of mAbs recognizing diferent pep-tide fragments. Using the individual anti-GDH anti-bodies as probes, the cross reactivities of brain tisues were investigated. For the human and ani-mal tissues tested, imunoreactive bands on Western blots appeared to have the same molec-ular mas of 55 kDa when hGHD60-6, hGHD60-8, or hGHD91-14 mAbs were used as probes. How-ever, the anti-human GDH mAbs imunoreactive to bands on Western blots reacted diferently on the imunoblots of the other animal brains tested, i.e., the two monoclonal antibodies hGDH63-10 and hGDH63-1 only produced positive results for human. These results suggest that human brain other mamalian brains. Thorough characterization of these anti-human GDH mAbs could provide potentially valuable tol as immunodiagnostic rea-gents for the detection, identification and charac-terization of the various neurological diseases re-lated to the GDH enzyme.

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