DNA polymerases from a parasitic protozoa Leishmania donovani UR6: evidence of presence of a novel kind of DNA polymerase.
DNA polymerases of Leishmania donovani have been isolated and purified. The cell extract has been chromatographed on a phosphocellulose column that separated into three peaks. The activity peak 1 was further purified to homogeneity. The DNA polymerase is a 64 KDa polypeptide, resistant to N-ethylmaleimide and aphidicolin. It requires MnCl2 and a high concentration of KCl (0.5 M) for maximal activity. It has both 3' to 5' and 5' to 3' exonuclease activities that reside in the same polypeptide.
Sen
S
S
Department of Molecular Parasitology, Indian Institute of Chemical Biology, Jadavpur, Calcutta, India.
Khalkho
N V
NV
Majumder
H K
HK
D000818:Animals; D002853:Chromatography, Liquid; D004261:DNA Replication; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification* / Q000378:metabolism; D004720:Endonucleases / Q000378:metabolism; D005092:Exonucleases / Q000378:metabolism; D007700:Kinetics; D007893:Leishmania donovani / Q000201:enzymology*
D004259:DNA-Directed DNA Polymerase; D004720:Endonucleases; D005092:Exonucleases