Cloning studies on the gene coding for L-(+)-lactate dehydrogenase of Plasmodium falciparum.
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 lambda gt11Tn5 expression library. DNA sequence analysis of one clone, lambda LDH-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.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D003001:Cloning, Molecular; D005796:Genes; D007770:L-Lactate Dehydrogenase / Q000032:analysis / Q000235:genetics*; D010963:Plasmodium falciparum / Q000201:enzymology / Q000235:genetics*
D000911:Antibodies, Monoclonal; D007770:L-Lactate Dehydrogenase