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J Med Microbiol 32 (1990), 1-7; DOI: 10.1099/00222615-32-1-1
© 1990 Society for General Microbiology
ISSN 0022-2615
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Expression of carbonic anhydrase in neisseriae and other heterotrophic bacteria

B. M. NAFI, R. J. MILES*, L. O. BUTLER1, N. D. CARTER1, C. KELLY{dagger} and S. JEFFERY{dagger}

Department of Microbiology, King's College, Campden Hill Road, London W8 7AH

{dagger}Departments of Child Health and Medical Microbiology, St George's Hospital Medical School, London SW17 ORE

* Correspondence should be sent to Dr R. J. Miles, Department of Microbiology, King's College, Campden Hill Road, London W8 7AH.

Received April 18, 1989 Revision received September 18, 1989.
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 N. sicca and N. gonorrhoeae. However, all Neisseria strains, including various isolates of N. meningitidis and N. lactamica, were sensitive to acetazolamide, when grown in air, and showed serological cross-reaction with N. sicca CA. Strains of other genera were resistant to acetazolamide. A number of strains including members of the genera Pseudomonas, Staphylococcus, Streptococcus, Serratia and Proteus 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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