| Literature DB >> 16143456 |
Rohana P Dassanayake1, Mark A Griep, Gerald E Duhamel.
Abstract
The cytolethal distending toxin B (CdtB) of the mouse pathogen Helicobacter hepaticus has cation binding and DNA catalysis residues in common with members of the mammalian deoxyribonuclease I (DNase I) family. The purpose of the present study was to characterize CdtB nuclease. To establish optimal digestion conditions and to evaluate co-factor requirements, a novel and sensitive fluorometric assay that quantitatively determines double stranded DNA digestion was developed. Although the Ca2+- and Mg2+-dependence and neutral properties of CdtB were similar to DNase I, hydrolysis of DNA by CdtB was approximately 100-fold less active than DNase I and was considerably more resistant to inhibition by ZnCl2 and G-actin.Entities:
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Year: 2005 PMID： 16143456 DOI： 10.1016/j.femsle.2005.08.005
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN： 0378-1097 Impact factor: 2.742