Polyclonal antisera raised against Plasmodium knowlesi reacted with (1) NADP-specific glutamate dehydrogenase (GLDH) of P. knowlesi, (2) GLDH of P. falciparum and (3) GLDH of Proteus spp. The antisera did not react with NAD(P) GLDH from bovine liver. Polyclonal antisera raised against the GLDH of Proteus spp. cross-reacted with GLDH from P. falciparum. Monoclonal antibodies (McAbs) obtained from mice immunized with Proteus GLDH were either specific for the bacterial enzyme or cross-reacted with P. falciparum GLDH. The selected McAbs did not react with GLDI-1 from P. knowlesi, P. chabaudi or P. berghei. The GLDH of P. falciparum was shown to be a cytosolic protein (by FAT) with a subunit molecular weight of approximately 49000 Da (by immunoprecipitation) having a pre dominantly hexameric form (by sucrose density gradient). Implications of the conserved sequences of GLDHs and other enzymes are discussed.
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