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Infect Immun. Jan 1986; 51(1): 352–354.
PMCID: PMC261110
Identification and preliminary characterization of external membrane-bound nuclease activities in Mycoplasma pulmonis.
F C Minion and J D Goguen
Mycoplasma pulmonis has substantial DNase activity exposed on the cell surface. At least part of this activity is attributable to an endonuclease. The activity is destroyed at 56 degrees C and inhibited by either 5 mM EDTA or 10 mM zinc chloride. It can also be eliminated by treatment of intact organisms with trypsin and is regenerated by incubation of the treated organisms in a medium that supports protein synthesis. DNase exposed at the cell surface constitutes 20% of the total DNase activity present in M. pulmonis extracts.
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