Abstract
Double immunodiffusion tests were performed with crude extracts from various Micrococcus species and antisera against catalase of Micrococcus luteus CCM 169. Cell-free extracts of M. lylae ATCC 27566 exhibited good cross-reaction. Cell-free extracts or catalase enriched preparations of M. varians reacted very weakly and no reaction has been found with preparations of M. kristinae, M. nishinomiyaensis, M. roseus and M. sedentarius. The quantitative microcomplement fixation assay also revealed a closer relationship between M. luteus and M. lylae than between M. luteus and M. varians. Strains of other Micrococcus species reacted in the microcomplement assay with M. luteus antiserum just as weakly as non-related strains, e.g. Staphylococcus aureus or Cellulomonas cartalyticum.
Similar content being viewed by others
References
Beers, R. F., Sizer, J. W.: A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. biol. Chem. 195, 133–140 (1952)
Champion, A. B., Prager, E. M., Wachter, D., Wilson, A. C.: Microcomplement fixation. In: Biochemical and immunological taxonomy of animals (C. A. Wright, ed.), pp. 397–416. London: Academic Press 1974
Champion, A. B., Soderberg, K. L., Wilson, A. C., Ambler, R. P.: Immunological comparison of azurins of known amino acid sequence. J. Mol. Evol. 5, 291–305 (1975)
Collins-Thompson, D. L., Sørhoug, T., Wilter, L. D., Ordal, Z. J.: Taxonomic consideration of Microbacterium lacticum. Microbacterium flavum and Microbacterium thermosphactum. Int. J. Syst. Bact. 22, 65–72 (1972)
Dayhoff, M. O.: Atlas of protein sequence and structure. 4th National Biochemical Research Foundation, Silver Spring, Maryland (1969)
DeLey, J., Kersters, K.: Biochemical evolution in bacteria. In: Comprehensive biochemistry, Vol. 29B (M. Florkin, E. H. Stotz, eds.), pp. 1–77. Amsterdam: Elsevier 1975
El-Sharkawy, T. A., Huisingh, D.: Differentiation among Xanthomonas species by polyacrylamide gel electrophoresis of soluble proteins. J. gen. Microbiol. 68, 155–165 (1971)
Gregory, E. M., Fridovich, J.: Visualization of catalase on acrylamide gels. Analyt. Biochem. 58, 57–62 (1974)
Hartree, E. F.: Determination of protein: A modification of the Lowry method that gives a linear photometric response. Analyt. Biochem. 48, 422–427 (1972)
Herbert, D.: Catalase from bacteria (Micrococcus lysodeikticus). In: Methods in enzymology, Vol. II (S. P. Colowick, N. O. Kaplan, eds.), pp. 784–788. London: Academic Press 1955
Kloos, W. E.: Transformation of Micrococcus lysodeikticus by various members of the family Micrococcaceae. J. gen. Microbiol. 59, 247–255 (1969)
Kloos, W. E., Tornabene, T. G., Schleifer, K. H.: Isolation and characterization of micrococci from human skin, including two new species: M. lylae and M. kristinae. Int. J. Syst. Bact. 24, 79–101 (1974)
Margoliash, E., Fitch, W. M.: The evolutionary information content of protein amino acid sequences. Miami Winter Symposium, Vol 1, pp. 33–51. Amsterdam: North-Holland 1970
Maurer, H. R.: Disc-electrophoresis and related techniques of polyacrylamide gel electrophoresis. Berlin: de Gruyter 1971
Nolan, C., Margoliash, R. E.: Comparative aspects of primary structures of protein. Ann. Rev. Biochem. 37, 727–790 (1968)
Ogasawara-Fujita, N., Sakaguchi, K.: Classification of micrococci on the basis of deoxyribonucleic acid homology. J. gen. Microbiol. 94, 97–106 (1976)
Ouchterlony, Ö.: Diffusion-in-gel methods for immunological analysis. Progr. Allergy 6, 30 (1962)
Prager, E. M., Wilson, A. C.: The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. I. Microcomplement fixation studies. J. biol. Chem. 246, 5978–5989 (1971a)
Prager, E. M., Wilson, A. C.: The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and microcomplement fixation results. J. biol. Chem. 246, 7010–7017 (1971b)
Ringelmann, R., Opferkuch, W., Röllinghoff, M., Loos, M.: Komplementmessung mit Hilfe des Mikrolitersystems. Z. med. Microbiol. Immunol. 154, 329–343 (1969)
Sarich, V. M.: Pinniped origins and the rate of evolution of carnivore albumin. Syst. Zool. 18, 286–295 (1969)
Schleifer, K. H., Schumacher-Perdreau, F., Götz, F., Popp, B., Hajek, V.: Chemical and biochemical studies for the differentiation of coagulase-positive staphylococci. Arch. Microbiol. 110, 263–270 (1976)
Swift, H. F., Wilson, A. T., Lancefield, R. C.: Typing group A hemolytic streptococci by M precipitin reactions in capillary pipettes. J. exp. Med. 78, 127–133 (1943)
Warburg, O., Christian, W.: Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z. 310, 384–421 (1942)
Whiteside, T. L., Desiervo, A. J., Salton, M. R. J.: Use of antibody to membrane adenosintriphosphatase in the study of bacterial relationships. J. Bact. 105, 957–967 (1971)
Williams, R. A. D., Sadler, S. A.: Electrophoresis of glucose-6-phosphate dehydrogenase, cell wall composition and the taxonomy of heterofermentative lactobacilli. J. gen. Microbiol. 65, 351–358 (1971)
Author information
Authors and Affiliations
Additional information
This work was supported by Deutsche Forschungsgemeinschaft
Rights and permissions
About this article
Cite this article
Rupprecht, M., Schleifer, KH. Comparative immunological study of catalases in the genus Micrococcus . Arch. Microbiol. 114, 61–66 (1977). https://doi.org/10.1007/BF00429631
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00429631