Deoxyribonucleic acid polymerase from the marine Pseudomonas sp. BAL-31.
A deoxyribonucleic acid (DNA)-dependent DNA polymerase (DNA nucleotidyltransferase) was purified 3,000-fold from the marine Pseuodomonas sp. BAL-31. The molecular weight of the native enzyme was estimated by glycerol gradient sedimentation to be 110,000. The enzyme migrated in sodium dodecyl sulfate-acrylamide gels as a single polypeptide with a molecular weight of 105,000. An absolute requirement for divalent cation was satisfied by Mg2+ or Mn2+ at concentrations of 1 mM. Monovalent cations at concentrations higher than 50 mM showed an inhibitory effect. The polymerase activity was resistant to N-ethylmaleimide and showed a wide pH optimum.
D004259:DNA-Directed DNA Polymerase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D012623:Seawater; D012965:Sodium Chloride / Q000494:pharmacology
D008345:Manganese; D012965:Sodium Chloride; D004259:DNA-Directed DNA Polymerase; D008274:Magnesium; D005033:Ethylmaleimide