1887

Abstract

Summary

A diverse range of heterotrophic bacteria was screened for the presence of carbonic anhydrase (CA) activity, sensitivity to inhibition of growth by acetazolamide (CA inhibitor), and the presence of protein binding monospecific antibody prepared against purified Neisseria sicca CA. CA activity was demonstrated only in strains of and However, all strains, including various isolates of and , were sensitive to acetazolamide, when grown in air, and showed serological cross-reaction with CA. Strains of other genera were resistant to acetazolamide. A number of strains including members of the genera and also strongly expressed a gene product(s) immunologically related to CA. The presence of CA cross-reacting proteins, which lack hydrase activity, is discussed in relation to the function of the various mammalian CA isoenzymes.

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1990-05-01
2022-01-26
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References

  1. Carter N, Jeffery S. Carbonic ahydrase: update and new horizons. Biochem Soc Trans 1985; 13:531–535
    [Google Scholar]
  2. Veitch F P, Blankenship L C. Carbonic anhydrase in bacteria. Nature 1963; 197:76–77
    [Google Scholar]
  3. Forkman A, Laurell A B. The effect of carbonic anhydrase inhibitor on the growth of neisseriae. Acta Pathol Microbiol Scand 1965; 65:450–456
    [Google Scholar]
  4. Sanders E, Maren T H. Inhibition of carbonic anhydrase in Neisseria: effects on enzyme activity and growth. Mol Pharmacol 1967; 3:204–215
    [Google Scholar]
  5. Forkman A. Inhibition by acetazolamide of the growth of neisseriae at increasing environmental concentration of CO2. Acta Pathol Microbiol Scand 1968; 73:298–302
    [Google Scholar]
  6. Berger U, Issi R. Resistenz gegen Acetazolamid alstaxonomische Kriterium bei Neisseria. Arch Hyg Bakteriol 1971; 154:540–544
    [Google Scholar]
  7. Main E R, Locke A. Carbonic anhydrase. III. Effect on growth of the Type I Pneumococcus, in vitro. J Bacteriol 1944; 48:77–81
    [Google Scholar]
  8. Shoaf W T, Jones M E L. Carbonic anhydrase of micro-organisms. I. An enzyme from baker’s yeast which catalyzes the formation of carbamate from ammonium bicarbonate solutions. Arch Biochem Biophys 1970; 139:130–142
    [Google Scholar]
  9. Gill S R, Fedorka-Cray P J, Tweten R K, Sleeper B P. Purification and properties of the carbonic anhydrase of Rhodospirillum rubrum. Arch Microbiol 1984; 138:113–118
    [Google Scholar]
  10. Yagawa Y, Shiraiwa Y, Miyachi S. Carbonic anhydrase from the blue-green alga (Cyanobacterium) Anabaena variabilis. Plant Cell Physiol 1984; 25:775–783
    [Google Scholar]
  11. Jahnke L S, Lyman C, Hooper A B. Carbonic anhydrase, carbon dioxide levels and growth of Nitrosomonas. Arch Microbiol 1984; 140:291–293
    [Google Scholar]
  12. Adler L, Brundell J, Falkbring S O, Nyman P O. Carbonic anhydrase from Neisseria sicca, strain 6021.1. Bacterial growth and purification of the enzyme. Biochim Biophys Acta 1972; 284:298–310
    [Google Scholar]
  13. Lowry O H, Rosebrough N J, Farr A L, Randall R J. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193:265–275
    [Google Scholar]
  14. Ouchterlony O. Diffusion-in-gel methods for immunological analysis. Prog Allerg 1962; 6:30–154
    [Google Scholar]
  15. Hawkes R, Niday E, Gordon J. A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem 1982; 119:142–147
    [Google Scholar]
  16. Nafi B M. Aspects of growth and carbonic anhydrase synthesis in Neisseria. PhD thesis, University of London 1987
    [Google Scholar]
  17. Forkman A. The location of carbonic anhydrase in a strain of Neisseria flava. Acta Pathol Microbiol Scand [B] 1972; 80:460–466
    [Google Scholar]
  18. MacLeod M N, De Voe I W. Localization of carbonic anhydrase in the cytoplasmic membrane of Neisseria sicca (strain 19). Can J Microbiol 1981; 27:87–92
    [Google Scholar]
  19. Okabe K, Yang S Y, Tsuzuki M, Miyachi S. Carbonic anhydrase: its content in spinach leaves and its taxonomic diversity studied with anti-spinach leaf carbonic anhydrase antibody. Plant Sci Lett 1984; 33:145–153
    [Google Scholar]
  20. Yang S Y, Tsuzuki M, Miyachi S. Carbonic anhydrase of Chlamydomonas: purification and studies on its induction using antiserum against Chlamydomonas carbonic anhydrase. Plant Cell Physiol 1985; 26:25–34
    [Google Scholar]
  21. Chapman S K, Maren T H. A search for the function of human carbonic anhydrase B. Biochim Biophys Acta 1978; 527:272–276
    [Google Scholar]
  22. Verpoorte J A, Mehta S, Edsall J T. Esterase activities of human carbonic anhydrases B and C. J Biol Chem 1967; 242:4221–4229
    [Google Scholar]
  23. Pocker Y, Sarkanen S. Carbonic anhydrase: structure, catalytic versatility, and inhibition. Adv Enzymol 1978; 47:149–274
    [Google Scholar]
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