Partial purification and characterization of a beta-like DNA polymerase from Leishmania mexicana.
Deoxyribonucleic acid polymerase beta (EC 2.7.7.7) from the lower eukaryotic parasitic protozoan Leishmania mexicana has been partially purified over 9,000 fold and characterized for the very first time. Like mammalian DNA polymerase beta the protozoan enzyme is of low molecular weight (40,000), has a broad pH range, and is resistant to inhibition by N-ethylmaleimide and aphidicolin. It is unlike mammalian DNA polymerase beta in utilization of various templates and response to various inhibitors and sensitivity to high ionic strength, but similar to a beta-like enzyme from a related organism Crithidia fasciculata. It is estimated that this enzyme constitutes 20% of the polymerase activity of the crude cell extract.
Nolan
L L
LL
School of Public Health, Morrill Science Center, University of Massachusetts, Amherst 01003.
Rivera
J H
JH
D000818:Animals; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D003429:Cross Reactions / Q000276:immunology; D004256:DNA Polymerase I / Q000187:drug effects / Q000302:isolation & purification*; D007894:Leishmania mexicana / Q000201:enzymology*; D008322:Mammals; D008970:Molecular Weight
D004256:DNA Polymerase I