Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/32792
標題: Recombinant pseudorabies virus DNase exhibits a RecBCD-like catalytic function
作者: Hsiang, C.Y.
張天傑
Ho, T.Y.
Hsiang, C.H.
Chang, T.J.
關鍵字: type-1 alkaline nuclease
aujeszkys-disease virus
staphylococcal
nuclease
binding protein
simplex
deoxyribonuclease
enzyme
gene
identification
purification
期刊/報告no:: Biochemical Journal, Volume 330, Page(s) 55-59.
摘要: The pseudorabies virus (PRV) DNase gene has previously been mapped within the PRV genome. To characterize further the enzymic properties of PRV DNase, this enzyme was expressed in Escherichia coli with the use of a pET expression vector. The protein was purified to homogeneity and assayed for nuclease activity in vitro. Recombinant PRV DNase exhibited an alkaline pH preference and an absolute requirement for Mg2+ ions that could not be replaced by Ca2+ and Na+ ions. Further studies showed that PRV DNase exhibited endonuclease, 5'-exonuclease and 3'-exonuclease activities in both single-stranded and double-stranded DNA. This activity occurred randomly and no significant base preference was demonstrated, The multiple biochemical activities of PRV DNase are similar to the activities of Neurospora crassa endo-exonuclease and E. coli RecBCD, two additional enzymes that are involved in recombination. Taken together, the similarity of action between N. crassa endo-exonuclease, E. coli RecBCD, and PRV DNase suggests that PRV DNase might have a role in the process of recombination that occurs during PRV infection.
URI: http://hdl.handle.net/11455/32792
ISSN: 0264-6021
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