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Antibodies to the glutamate dehydrogenase of Plasmodium falciparum

Published online by Cambridge University Press:  06 April 2009

I. T. Ling ,
S. Cooksley ,
P. A. Bates ,
E. Hempelmann  and
R. J. M. Wilson
I. T. Ling
Affiliation:
National institute for Medical Research, Mill Hill, London
S. Cooksley
Affiliation:
Brunel University, Department of Applied Biology, Uxbridge, Middlesex
P. A. Bates
Affiliation:
National institute for Medical Research, Mill Hill, London
E. Hempelmann
Affiliation:
Institut für Biochemie II, Im Neuenheimer Feld 328 D-6900, Heidelberg 1, FRG
R. J. M. Wilson
Affiliation:
National institute for Medical Research, Mill Hill, London
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Summary

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.

Type
Research Article
Information
Parasitology , Volume 92 , Issue 2 , April 1986 , pp. 313 - 324
Copyright
Copyright © Cambridge University Press 1986

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