Properties of the major non-specific endonuclease from the strict anaerobe Fibrobacter succinogenes and evidence for disulfide bond formation in vivo.

@article{Maclellan2001PropertiesOT,
  title={Properties of the major non-specific endonuclease from the strict anaerobe Fibrobacter succinogenes and evidence for disulfide bond formation in vivo.},
  author={Shawn R Maclellan and Cecil W. Forsberg},
  journal={Microbiology},
  year={2001},
  volume={147 Pt 2},
  pages={
          315-23
        }
}
DNase A is a non-specific endonuclease of Fibrobacter succinogenes. The enzyme was purified to homogeneity and its properties studied both in vitro and in vivo. Magnesium but not calcium was essential for nucleolytic activity. Manganese ions substituted for magnesium but were less stimulatory. DNase A activity was markedly inhibited by either NaCl or KCl at concentrations greater than 75 mM. The enzyme had a temperature optimum of 25 degrees C and a pH optimum of about 7.0. Values for K:(m) and… 
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