Open AccessTWO DEOXYRIBONUCLEASE ACTIVITIES WITHIN PURIFIED VACCINIA VIRUS
Author(s) -
Beatriz G.T. Pogo,
Samuel Dales
Publication year - 1969
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.63.3.820
Subject(s) - vaccinia , endonuclease , deoxyribonuclease , virus , exonuclease , dna , deoxyribonucleases , enzyme , chemistry , poxviridae , virology , deoxyribonuclease i , exonuclease iii , biology , biochemistry , recombinant dna , escherichia coli , base sequence , dna polymerase , gene
Two DNases, both hydrolizing single-stranded DNA, were identified within highly purified particles of vaccinia virus. One of these, active optimally at pH 5.0, is an exonuclease and the other, most active at pH 7.8, is an endonuclease. These two activities were localized more specifically within the virus cores. Upon elimination of the envelopes, followed by removal of the lateral bodies of vaccinia, both DNases were activated, suggesting that a specific inhibitor of these enzymes may be present in the lateral bodies.
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