作者: P Modrich , C C Richardson
DOI: 10.1016/S0021-9258(19)41212-X
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摘要: The DNA polymerase induced after infection of Escherichia coli by phage T7 has been purified 500-fold to near homogeneity as judged polyacrylamide gel electrophoresis in the presence sodium dodecyl sulfate. enzyme complements extracts cells infected with a gene 5 mutant permit cell-free replication duplex DNA. In contrast, T4 or E. I is unable do so, thus suggesting specific requirement for viral TsnC protein present one-to-one stoichiometry protein, and can be isolated homogeneous form from heat-denatured chromatography on DEAE-cellulose. inactive that accumulates tsnC hosts partially purified. When mixed activity restored, formation complex between two proteins occurs. These results indicate functional ofT7 composed phage- host-specified subunits.