A comparative biochemical study of virus-induced DNA polymerases was made among the herpes group viruses: namely, herpes simplex virus (HSV) type 1 and type 2, human cytomegalovirus (HCMV) and varicella-zoster virus (VZV). Although these virus-induced enzymes shared some biochemical properties, they differed in several important aspects. All these virus-induced DNA polymerases could efficiently use poly(dC) · oligo(dG)i2-i8 and poly(dA) · oligo(dT)i2-i8 as template-primers. However, in phosphocellulose chromatography, HSV-1-and HSV-2-induced enzymes were eluted at the low concentration of 0.18–0.20 M NaCl and the counterparts of HCMV and VZV were eluted at 0.30–0.32 M. The former two enzymes were more sensitive to lower concentrations of phosphonoacetate and ethyl phosphonoacetate than the latter two enzymes. Moreover, the activity of HSV-1- and HSV-2-specified DNA polymerases was 5 times greater in the presence of 60 mM ammonium sulfate if poly(dA) · oligo(dT)i2-i8 was used as template-primer, while HCMV- and VZV-induced enzyme activities were only about twice as great under the same conditions. Furthermore, DNase activity was conspicuous in both HSV-1- and HSV-2-infected WI-38 cells, but was not detectable in HCMV-and VZV-infected cells. After storage for 1 year at 4°, the HSV-1-induced DNA polymerase was the most thermostable of the four viral enzymes.

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