Isolation and partial characterization of DNA polymerases from Crithidia fasciculata.
Two types of DNA polymerase activity were partially purified from Crithidia fasciculata. The alpha-type, DNA polymerase A, was of high molecular weight and sensitive to N-ethylmaleimide, whereas the beta-type, DNA polymerase B, was of low molecular weight and resistant to N-ethylmaleimide. Phosphocellulose chromatography revealed multiple peaks of DNA polymerase A activity the properties of which, such as pH optimum, salt sensitivity, utilization of synthetic template-initiator complexes and response to DNA polymerase inhibitors were similar. The response of the C. fasciculata DNA polymerase A enzymes to some of these inhibitors and utilization of poly(rA) X oligo(dT)11 showed these enzymes to be markedly different from mammalian DNA polymerase alpha.
D000818:Animals; D002845:Chromatography; D003421:Crithidia / Q000201:enzymology*; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification*; D005033:Ethylmaleimide / Q000494:pharmacology; D007526:Isoelectric Point; D008970:Molecular Weight; D013698:Templates, Genetic
D004259:DNA-Directed DNA Polymerase; D005033:Ethylmaleimide