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

Infection and Immunity
F C Minion, J D Goguen

Abstract

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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Citations

Oct 1, 1994·AIDS Research and Human Retroviruses·C QuillentA Blanchard
Sep 21, 2019·Scientific Reports·Fabien RideauCécile Bébéar
Jan 11, 2012·Nucleic Acid Therapeutics·Frank J HernandezJames O McNamara
Aug 24, 1999·Infection and Immunity·M BendjennatE Bahraoui
Dec 19, 2019·Frontiers in Microbiology·Xifang ZhuEric Baranowski
Apr 1, 1997·Journal of Bacteriology·M BendjennatE Bahraoui
Dec 1, 1993·Journal of Bacteriology·F C MinionE Tigges

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