Particulate DNA polymerase from the cytoplasm of Xenopus laevis oocytes.
A DNA polymerase has been partially purified and characterized from Xenopus laevis stage 6 oocytes. The enzyme is present only in the cytoplasm and has been shown to be able to copy Poly(A) x oligo(dT), to be sensitive to N-ethylmaleimide, and to sediment faster than 4 S in high salt glycerol gradient. The enzyme can be extracted from particulate material which has a density in sucrose gradient ranging from 1.200 to 1.225 g/cc. This particulate material is identified by its ability to use Poly(A) x oligo(dT) as template in an exogenous DNA polymerase reaction and by its endogenous DNA synthesizing capacity.
Baldi
M I
MI
Laboratory of Cell Biology, C. N. R., Via Romagnosi 18A, 00196 Rome, Italy.
Bazzicalupo
P
P
Tocchini-Valentini
G P
GP
D000818:Animals; D002499:Centrifugation, Density Gradient; D002848:Chromatography, DEAE-Cellulose; D003593:Cytoplasm / Q000201:enzymology*; D004247:DNA / Q000096:biosynthesis; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D019384:Nucleic Acid Synthesis Inhibitors; D009865:Oocytes / Q000201:enzymology*; D011189:Potassium Chloride / Q000494:pharmacology; D014982:Xenopus laevis
D019384:Nucleic Acid Synthesis Inhibitors; D011189:Potassium Chloride; D004247:DNA; D004259:DNA-Directed DNA Polymerase; D005033:Ethylmaleimide