[The chromatographic properties of the DNA-dependent DNA polymerases from Acholeplasma laidlawii PG-8].
The DNA-dependent DNA-polymerase (DNA polymerase I which is not sorbed on the column with DEAE-cellulose, and DNA-polymerase II, which is absorbed by this column and is eluted from it by 0.3 M of NaCl), have been isolated from Acholeplasma laidlawii PG-8. DNA-polymerase I in homogeneous state was obtained as a result of the stepwise treatment by heparin-sepharose (elution at 0.35 M of NaCl) and poly-U-sepharose (elution at 0.3 M of NaCl). It was presented on the electrophoregram by one polypeptide with molecular weight of 72 kDalton. The second form of DNA polymerase was also obtained in homogeneous state as a result of sequential treatment on heparin-sepharose (elution at 0.3 M of NaCl) and on poly-A-sepharose (elution at 0.25 M of NaCl): the protein which had manifested polymerase activity was a polypeptide with molecular weight of 45 kDalton.
Bezuglyĭ
S V
SV
Skripal'
I G
IG
Babichev
V V
VV
D000128:Acholeplasma laidlawii / Q000201:enzymology*; D002847:Chromatography, Agarose / Q000379:methods; D004259:DNA-Directed DNA Polymerase / Q000032:analysis / Q000302:isolation & purification*; D004586:Electrophoresis; D008970:Molecular Weight
D004259:DNA-Directed DNA Polymerase
Khromatograficheskie svoĭstva DNK-zavisimykh DNK-polimeraz iz Acholeplasma laidlawii PG-8.