Cellular distribution, purification and electrophoretic properties of malate dehydrogenase in Trichuris ovis and inhibition by benzimidazoles and pyrimidine derivatives.
High levels of malate dehydrogenase were found in Trichuris ovis. Two molecular forms of the enzyme, of different cellular location and electrophoretic pattern, were isolated and purified. The activity of soluble malate dehydrogenase was greater than that of mitochondrial malate dehydrogenase. Both forms also displayed different electrophoretic profiles in comparison with purified extracts from goat (Capra hircus) liver. Substrate concentration directly affected enzyme activity. Host and parasite malate dehydrogenase activity were both inhibited by a series of benzimidazoles and pyrimidine-derived compounds, some of which markedly reduced parasite enzyme activity, but not host enzyme activity. Percentage inhibition by some pyrimidine derivatives was greater than that produced by benzimidazoles.
Sanchez-Moreno
M
M
Instituto López-Neyra de Parasitología, C.S.I.C., Granada, Spain.
Ortega
J E
JE
Valero
A
A
D000818:Animals; D001562:Benzimidazoles / Q000494:pharmacology*; D002850:Chromatography, Gel; D004592:Electrophoresis, Starch Gel; D006041:Goats; D007527:Isoenzymes / Q000032:analysis; D008099:Liver / Q000201:enzymology; D008291:Malate Dehydrogenase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D008293:Malates / Q000378:metabolism; D015394:Molecular Structure; D011743:Pyrimidines / Q000494:pharmacology*; D013379:Substrate Specificity; D014258:Trichuris / Q000201:enzymology*
D001562:Benzimidazoles; D007527:Isoenzymes; D008293:Malates; D011743:Pyrimidines; C030298:malic acid; D008291:Malate Dehydrogenase