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Antibodies to the glutamate dehydrogenase of Plasmodium falciparum.

Polyclonal antisera raised against Plasmodium knowlesi reacted with NADP-specific glutamate dehydrogenase ( GLDH) of P. knowlesi, GLDH of P. falciparum and 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 GLDH 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 49 000 Da (by immunoprecipitation) having a predominantly hexameric form (by sucrose density gradient). Implications of the conserved sequences of GLDHs and other enzymes are discussed.[1]

References

  1. Antibodies to the glutamate dehydrogenase of Plasmodium falciparum. Ling, I.T., Cooksley, S., Bates, P.A., Hempelmann, E., Wilson, R.J. Parasitology (1986) [Pubmed]
 
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