Demonstration of a herpes simplex virus type 2-induced deoxyuridine triphosphate nucleotidohydrolase in infected KB cells and in biochemically transformed HeLa cells.
The deoxyuridine triphosphate nucleotidohydrolase (dUTPase) activity which is induced in KB cells infected with herpes simplex virus type 2 (HSV-2) and expressed in biochemically transformed HeLa cells was separated from the host dUTPase activity using either gel filtration or chromatofocusing chromatography. The HSV-2-induced dUTPase differed from the host dUTPase activity in its molecular weight (53000 versus 46000) and isoelectric point (pI 5 X 9 versus 6 X 4). However, it was similar to the host enzyme in that only dUTP served as a substrate for the enzyme.
D002472:Cell Transformation, Viral; D002850:Chromatography, Gel; D004790:Enzyme Induction; D006367:HeLa Cells / Q000201:enzymology / Q000382:microbiology*; D006561:Herpes Simplex / Q000201:enzymology / Q000382:microbiology*; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011755:Pyrophosphatases / Q000378:metabolism*; D018139:Simplexvirus / Q000201:enzymology*; D014776:Virus Cultivation
D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase