Abstract
As phospholipases of mycoplasma species may play a role in the pathogenesis of respiratory tract and urogenital tract diseasesMycoplasma mycoides andAcholeplasma laidlawii were examined as to the production of phospholipase A2 (PLA) and attempts were made to purify and characterize it. Both species produced PLA. The purified enzyme was found to be heat-labile, active at alkaline pH, revealing a single band in polyacrylamide gel electrophoresis. Metal ions such as calcium and barium, increased its activity whereas solvents at high concentrations decreased it. It was resistant to surfactants.
Similar content being viewed by others
References
Ames G.F.: Lipids ofSalmonella typhimurium andEscherichia coli: Structure and metabolism.J. Bacteriol. 95, 833–843 (1968).
Bartleit G.R.: Phosphorus assay in column chromatography.J. Biol. Chem. 234, 466–468 (1959).
Chanock R.M., Hayflick L., Barile M.F.: Growth on artificial medium of an agent associated with atypical pneumonia and its identification as a PPLO.Proc. Nat. Acad. Sci. 48, 41–48 (1962).
Cooper T.G.:Electrophoresis, inTools of Biochemistry, p. 194. John Willey and Sons, New York 1977.
Desilva N.S., Quinn P.A.: Endogenous activity of phospholipase A and C inUreaplasma urealyticum.J. Clin. Microbiol. 12, 354–358 (1986).
Doi O., Nojima S., Ohki M.: Two kinds of phospholipase A lysophospholipase inEscherichia coli.Biochim. Biophys. Acta 260, 249–258 (1972).
Embree J.E., Krause V.W., Embil J.A., MacDonald S.: Placental infection withMycoplasma hominis andUreaplasma urealyticum: Clinical correlation.Obstet. Gynecol. 56, 475–481 (1980).
Fung C.K., Proulx P.: Metabolism of phosphoglycerides inEscherichia coli. III. Presence of phospholipase A and A2 inEscherichia coli.Canad. J. Biochem. 47, 371–373 (1969).
Gross Z., Rottem S.: The preservation ofMycoplasma carpricolum cell inactness after phospholipase A2 treatment.Biochim. Biophys. Acta 778, 372–378 (1984).
Haberman E., Hardetk L.: A sensitive and specific plate test for the quantification of phospholipases.Ann. Biochem. 50, 163–173 (1972).
Ispolatorskaya M.V.: pp. 109–158 inMicrobial Toxins, Vol. II (Ed. S. Kadis, T. C. Montie, Ajil, Montie). Academic Press, New York-London 1971.
Kent C., Lennasz W.J.: An osmotically fragile mutant ofBacillus subtilis with an active membrane associated phospolipase A.Proc. Nat. Acad. Sci. 69, 2793–2797 (1972).
Lehmann V.: The nature of phospholipase C fromAcinetobacter calcoacelicous. Effects on whole red cells and red cell membranes.Acta Path. Microbiol. Scand. Sect. B 81, 419–421 (1973).
Linkisch P.G., Vogt W.: Direct hemolytic activity of phospholipase A.Biochim. Biophys. Acta 270, 241–247 (1972).
Magee W.L., Thompsen R.H.B.: The estimation of phospholipase A activity in aqueous systems.Biochem. J. 77, 526–534 (1960).
Magnusson B.J., Docry H.M., Gulasekharam J.: Phospholipase activity of staphylococcal toxin.Nature 196, 270–273 (1962).
Miller G.L.: Use of dinitrosalicylic acid for determination of reducing sugars.Anal. Chem. 31, 426–428 (1959).
Nygren B., Hoborn J., Wahlen P.: Phospholipase A production inStaphylococcus aureus.Acta Path. Microbiol. Scand. 68, 429–433 (1966).
Okama Y., Yamaguchi T.: Studies on phospholipase fromStreptomyces purification and properties ofStreptomyces lachiyoenhis phospholipase D.J. Biochem. 78, 363–373 (1975).
Ono Y., Nojima S.: Phospholipase of the membrane fraction ofMycobacterium phlei.Biochim. Biophys. Acta 76, 111–119 (1969).
Pasten I., Macchina V., Katsen R.: A phospholipase specific for sphingomyelin fromClostridium perfringens.J. Biol. Chem. 243, 3750–3755 (1968).
Proulx P.R., Van Deenen L.L.M.: Phospholipase activities ofEscherichia coli.Biochim. Biophys. Acta 144, 171–174 (1967).
Quinn P.A., Butamy J., Chimpora M., Taylor J., Mannal W.: Prospective study of microbial infection in still births and early neonatal death.Am. J. Obstet. Gynecol. 151, 238–249 (1985).
Randerath K.:Thin Layer Chromatography. Springer Verlag, Berlin 1965.
Rao R.H., Subrahmanyam D.: Studies on the phospholipase A in larvae ofCulex pipiens fatigans.J. Insect. Physiol. 15, 149–153 (1961).
Raybin D.M., Bertsch L.L., Kornberg A.: A phospholipase inBacillus megaterium unique to spores and sporangia.Biochemistry 11, 1754–1760 (1972).
Rottem S., Hasin M., Razin S.: Difference in susceptibility to phospholipase C of free and membrane bound phospholipids ofMycoplasma hominis.Biochim. Biophys. Acta 323, 520–531 (1973).
Scherizen J.J., Van Groningenen, Luyben W.A.H.H.: Phospholipase C fromBacillus cereus andClostridium welchi.Biochim. Biophys. Acta 649, 1–12 (1981).
Sneff L.M., Wagener W.S., Brooks G.F., Finnerty W.R., Makula K.A.: Phospholipids composition of phospholipase A ofNeisseria gonorrhoeae.J. Bacteriol. 127, 874–880 (1976).
Sonoki S., Ikezawa H.: Studies on phospholipase C fromPseudomonas aureofaciens: Purification and some properties of phospholipase C.Biochim. Biophys. Acta 403, 412–424 (1975).
Stanier R., Palleroni N.J., Doudoroff M.: The aerobicPseudomonas, a taxonomic study.J. Gen-.Microbiol. 43, 159–271 (1966).
Van Golde L.M.C., McElhaney R.N., Van Deenen L.L.M.: A membrane bound lysophospholipase fromMycoplasma laidlawii strain B.Biochim. Biophys. Acta 231, 245–249 (1971).
Verkleij A.J., Zwall R.F.A., Roelofsen B., Comfurius P., Kastelinjn D., Van Deenen L.L.M.: The asymmetric distribution of phospholipids in human red cell membrane. A combined study using phospholipases and freeze-etching electron microscopy.Biochim. Biophys. Acta 323, 178–193 (1973).
Writlind B., Heden L., Sjoberg L., Wadstrom C.: Production of enzymes and toxins by hospital strain ofPseudomonas aeruginosa in relation to serotypes and phage typing pattern.J. Med. Microbiol. 6, 91–100 (1973).
Zwaal R.F.A., Roelofsen B., Compfurius P., Van Deenen L.L.M.: Organization of phospholipids in human red cell membranes as detected by the action of various purified phospholipases.Biochim. Biophys. Acta 406, 83–86 (1975).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bhandari, S., Asnani, P.J. Characterization of phospholipase A2 of mycoplasma species. Folia Microbiol 34, 294–301 (1989). https://doi.org/10.1007/BF02814471
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02814471