DNA-dependent RNA polymerase from bacteriophage N4 virions. Purification and characterization.
作者： S.C. Falco , W. Zehring , L.B. Rothman-Denes
DOI: 10.1016/S0021-9258(19)85670-3
关键词:
摘要: A DNA-dependent RNA polymerase has been purified to homogeneity from bacteriophage N4 virions. Sodium dodecyl sulfate-8 M urea polyacrylamide gel electrophoresis of the enzyme revealed a single polypeptide with molecular weight 350,000. The hydrodynamic properties have determined be 9.5 S for sedimentation coefficient and 84 Stokes radius. These two parameters indicate native 320,000. Enzyme activity is dependent on presence Mg2+, four ribonucleoside triphosphates, denatured DNA. Under these conditions, initiation synthesis occurs exclusively pppG. inhibited by monovalent salts resistant drugs rifampicin streptolydigin. protein present in 1 2 copies per virion; its provides an explanation independence early host polymerase.
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