Identification and preliminary characterization of external membrane-bound nuclease activities in Mycoplasma pulmonis.

Infection and Immunity
F C Minion, 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.


Jun 1, 1978·Microbiological Reviews·S Razin
Jan 1, 1983·Methods in Enzymology·H C Birnboim
Oct 1, 1982·Journal of Bacteriology·J D Pollack, P J Hoffmann
Sep 1, 1965·Journal of Bacteriology·J D PollackR C Cleverdon

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