The DNA polymerases of Leishmania mexicana.
Two previously isolated DNA polymerases from the parasitic protozoan Leishmania mexicana were further characterized by exposure to inhibitors of mammalian DNA polymerases. DNA polymerase A, a high molecular mass enzyme, and DNA polymerase B, a beta-like DNA polymerase were compared to each other and to their mammalian counterparts regarding pH optimum, utilization of templates, and response to various inhibitors and ionic strengths. The results suggest that the DNA polymerases from L. mexicana differ from the host enzymes and may offer a target for chemotherapeutic intervention.
Nolan
L L
LL
University of Massachusetts, School of Public Health, Amherst 01003.
Rivera
J H
JH
D000818:Animals; D004256:DNA Polymerase I / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D004258:DNA Polymerase III / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007894:Leishmania mexicana / Q000201:enzymology*; D008970:Molecular Weight; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013698:Templates, Genetic
D012965:Sodium Chloride; D011189:Potassium Chloride; C065639:DNA polymerase A; D004256:DNA Polymerase I; D004258:DNA Polymerase III