Nonstructural proteins of herpes simplex virus. I. Purification of the induced DNA polymerase.
Herpes simplex virus-induced DNA polymerase purified by published methods was found to be contaminated with many others proteins, including virus structural proteins. Thus, DEAE-cellulose and phosphocellulose chromatography were used in combination with affinity chromatography to purify DNA polymerase from herpes simplex virus type 1- and type 2-infected cells. The purified enzyme retained unique features of the herpesvirus-induced DNA polymerase, including a requirement for high salt concentrations for maximal activity, a sensitivity to low phosphonoacetate concentrations, and the capacity to be neutralized by rabbit antiserum to herpesvirus-infected cells. By polyacrylamide gel electrophoresis, the purified DNA polymerase was associated with a virus-induced polypeptide of about 150,000 molecular weight.
D000914:Antibodies, Viral; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002460:Cell Line; D004259:DNA-Directed DNA Polymerase / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D003851:Deoxyribonucleases / Q000096:biosynthesis; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009500:Neutralization Tests; D010746:Phosphonoacetic Acid / Q000494:pharmacology; D018139:Simplexvirus / Q000032:analysis* / Q000276:immunology
D000914:Antibodies, Viral; D001426:Bacterial Proteins; D004259:DNA-Directed DNA Polymerase; D003851:Deoxyribonucleases; D008274:Magnesium; D010746:Phosphonoacetic Acid