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    Rights statement: http://journals.cambridge.org/action/displayJournal?jid=PAR The final, definitive version of this article has been published in the Journal, Parasitology, 92 (2), pp 313-324 1986, © 1986 Cambridge University Press.

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Antibodies to the glutamate dehydrogenase of Plasmodium falciparum

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Antibodies to the glutamate dehydrogenase of Plasmodium falciparum. / Ling, I T; Cooksley, S; Bates, P A et al.
In: Parasitology, Vol. 92, No. 2, 1986, p. 313-324.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Ling, IT, Cooksley, S, Bates, PA, Hempelmann, E & Wilson, RJ 1986, 'Antibodies to the glutamate dehydrogenase of Plasmodium falciparum', Parasitology, vol. 92, no. 2, pp. 313-324. https://doi.org/10.1017/S0031182000064088

APA

Ling, I. T., Cooksley, S., Bates, P. A., Hempelmann, E., & Wilson, R. J. (1986). Antibodies to the glutamate dehydrogenase of Plasmodium falciparum. Parasitology, 92(2), 313-324. https://doi.org/10.1017/S0031182000064088

Vancouver

Ling IT, Cooksley S, Bates PA, Hempelmann E, Wilson RJ. Antibodies to the glutamate dehydrogenase of Plasmodium falciparum. Parasitology. 1986;92(2):313-324. doi: 10.1017/S0031182000064088

Author

Ling, I T ; Cooksley, S ; Bates, P A et al. / Antibodies to the glutamate dehydrogenase of Plasmodium falciparum. In: Parasitology. 1986 ; Vol. 92, No. 2. pp. 313-324.

Bibtex

@article{92d21b65aba14ccd8f7f6efa91e12ead,
title = "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum",
abstract = "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.",
author = "Ling, {I T} and S Cooksley and Bates, {P A} and E Hempelmann and Wilson, {R J}",
note = "http://journals.cambridge.org/action/displayJournal?jid=PAR The final, definitive version of this article has been published in the Journal, Parasitology, 92 (2), pp 313-324 1986, {\textcopyright} 1986 Cambridge University Press.",
year = "1986",
doi = "10.1017/S0031182000064088",
language = "English",
volume = "92",
pages = "313--324",
journal = "Parasitology",
issn = "0031-1820",
publisher = "Cambridge University Press",
number = "2",

}

RIS

TY - JOUR

T1 - Antibodies to the glutamate dehydrogenase of Plasmodium falciparum

AU - Ling, I T

AU - Cooksley, S

AU - Bates, P A

AU - Hempelmann, E

AU - Wilson, R J

N1 - http://journals.cambridge.org/action/displayJournal?jid=PAR The final, definitive version of this article has been published in the Journal, Parasitology, 92 (2), pp 313-324 1986, © 1986 Cambridge University Press.

PY - 1986

Y1 - 1986

N2 - 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.

AB - 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.

U2 - 10.1017/S0031182000064088

DO - 10.1017/S0031182000064088

M3 - Journal article

C2 - 3086819

VL - 92

SP - 313

EP - 324

JO - Parasitology

JF - Parasitology

SN - 0031-1820

IS - 2

ER -