PMID: 2119590Aug 1, 1990Paper

Glycosidase activities of mycoplasmas

Zentralblatt Für Bakteriologie : International Journal of Medical Microbiology
I KahaneS Yatziv

Abstract

The activities of alpha- and beta-glucosidase, beta-galactosidase and beta-N acetylglucosaminidase were assessed at acidic pH by fluorimetry using the appropriate 4-methylumbelliferyl substrate in four Mycoplasma species (M. pneumoniae, M. gallisepticum, M. hominis and M. capricolum) and in Acholeplasma laidlawii. The glycosidase activities were in a low range (0.1-4.2 nmole per h per mg protein) with the exception of higher activities of beta-N-acetylglucosaminidase in A. laidlawii. The enzyme levels of a virulent and a nonvirulent strain of M. pneumoniae were comparable. Despite the very sensitive assay, neuraminidase activity was not detected in M. pneumoniae and M. gallisepticum. No induction of alpha-glucosidase could be demonstrated for M. pneumoniae or A. laidlawii. At least part of the glycosidase activities was localized in the membrane fraction of all mycoplasmas studied. This may support the hypothesis that pathogenic mycoplasmas, being membrane parasites, may modify, by their glycosidases, some host cell glycoconjugates. However, our study did not distinguish the pathogenic mycoplasmas to possess a characteristic glycosidase profile.

References

Nov 15, 1977·Biochimica Et Biophysica Acta·I Kahane, S Razin
Jan 27, 1971·Nature: New Biology·M L Slater, C E Folsome
Feb 15, 1980·Biochimica Et Biophysica Acta·I KahaneE A Rachmilewitz

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Citations

Jun 4, 2004·Journal of Bacteriology·D R BrownW G Farmerie
Feb 7, 2008·Avian Diseases·Meghan MayDaniel R Brown
Sep 1, 1991·Microbiological Reviews·M ManafiS Bascomb
Mar 29, 2008·Veterinary Microbiology·Rebeka Lucijana BercicDusan Bencina
Feb 10, 2009·Veterinary Microbiology·Meghan May, Daniel R Brown

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