title: Identification and preliminary characterization of external membrane-bound nuclease activities in Mycoplasma pulmonis.
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.
mesh_terms: D002462:Cell Membrane / Q000201:enzymology; D003851:Deoxyribonucleases / Q000378:metabolism*; D009174:Mycoplasma / Q000201:enzymology*; D014357:Trypsin / Q000378:metabolism
chemical_list: D003851:Deoxyribonucleases; D014357:Trypsin