Characterization of lactate dehydrogenase of Plasmodium knowlesi.
Some properties of purified lactate dehydrogenase, (EC. 1.1.1.27) from schizonts of Plasmodium knowlesi are described. The plasmodial enzyme migrated as single entity on polyacrylamide gel, and resembled rabbit muscle (M4) lactate dehydrogenase in its electrophoretic mobility. The P. knowlesi enzyme consisted of four identical subunits of 31 kDa. Purified lactate dehydrogenase was inhibited almost completely when incubated with 100 microM p-chloromercuribenzoate, Ag+ or Hg+ and such inhibition could be reversed by the addition of beta-mercaptoethanol or L-cysteine. Metal chelators did not show any remarkable effect. Oxalic acid is a competitive inhibitor of pyruvate reduction by this enzyme with apparent Ki of approximately equal to 0.41 mM.
D000818:Animals; D002412:Cations; D002614:Chelating Agents / Q000494:pharmacology; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D010070:Oxalates / Q000494:pharmacology; D019815:Oxalic Acid; D010961:Plasmodium / Q000201:enzymology*; D011487:Protein Conformation; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D002412:Cations; D002614:Chelating Agents; D010070:Oxalates; D013439:Sulfhydryl Reagents; D019815:Oxalic Acid; D007770:L-Lactate Dehydrogenase