title: Binding of deoxyribonucleic acid-dependent deoxyribonucleic acid polymerase to poxvirus.
abstract: Poxvirus has a deoxyribonucleic acid polymerase activity that remains associated with the virus despite repeated centrifugation through sucrose gradients. Highly purified poxvirus preparation can adsorb deoxyribonucleic acid polymerase from cytoplasmic extracts of cells containing such an activity. These results indicate that caution must be used in assuming that an enzyme associated with a purified virus is necessarily an integral part of the virion.
mesh_terms: D000327:Adsorption; D000818:Animals; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D006224:Cricetinae; D046508:Culture Techniques; D004247:DNA; D004254:DNA Nucleotidyltransferases / Q000032:analysis / Q000378:metabolism*; D004267:DNA Viruses / Q000201:enzymology / Q000254:growth & development / Q000302:isolation & purification; D005467:Floxuridine / Q000494:pharmacology; D006367:HeLa Cells; D006358:Hot Temperature; D006801:Humans; D007668:Kidney; D009691:Nucleic Acid Denaturation; D011212:Poxviridae / Q000201:enzymology*; D012487:Salmonidae; D013395:Sucrose; D013501:Surface-Active Agents; D013942:Thymine Nucleotides / Q000378:metabolism; D014316:Tritium; D014616:Vaccinia virus / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification
chemical_list: D013501:Surface-Active Agents; D013942:Thymine Nucleotides; D005467:Floxuridine; D014316:Tritium; D013395:Sucrose; D004247:DNA; D004254:DNA Nucleotidyltransferases