Cloning studies on the gene coding for l-(+)-lactate dehydrogenase of Plasmodium falciparum

David Ll Simmons, John E. Hyde, Martin Mackay, Mike Goman, John Scaife

    Research output: Contribution to journalArticlepeer-review

    Abstract

    We show that the l-(+)-lactate dehydrogenase (EC 1.1.1.27; l-lactate; NAD+-oxidoreductase) of Plasmodium falciparum (LDH-P) is encoded in the parasite genome. A monoclonal antibody (McAb 7.2) has been shown to bind the LDH-P subunit which has an apparent molecular mass of 35 kDa. A polyclonal antiserum raised against affinity purified LDH-P has been used to isolate cDNA clones containing LDH-P epitopes from a λgt11Tn5 expression library. DNA sequence analysis of one clone, λLDH-P.1, reveals a single open reading frame which shows a degree of homology to the N-terminal domain of known LDH amino acid sequences. © 1985.
    Original languageEnglish
    Pages (from-to)231-243
    Number of pages12
    JournalMolecular and biochemical parasitology
    Volume15
    Issue number2
    DOIs
    Publication statusPublished - May 1985

    Keywords

    • l-(+)-Lactate dehydrogenase
    • LDH clones
    • Malaria
    • Parasite enzymes
    • Plasmodium falciparum

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