PMID: 641210Apr 1, 1978Paper

Fluorimetric assay of mycobacterial group-specific hydrolase enzymes

Journal of Clinical Pathology
J M Grange

Abstract

Fluorigenic substrates prepared from 4-methylumbelliferone provide a simple, convenient method for detecting and assaying group-specific hydrolase activity in small quantities of whole mycobacteria. Physico-chemical properties of the enzymes such as pH dependence and heat stability may also be studied. A technique is described for studying glycosidase, hexosaminidase, acid phosphatase, and acyl esterase activity in seven mycobacterial species. Such techniques will be a useful aid to the taxonomy, identification, and quantification of mycobacteria, especially slowly growing strains in which biochemical properties are very difficult to detect by other techniques.

References

Feb 1, 1977·Journal of Clinical Pathology·J M Grange, K Clark
Mar 1, 1968·The American Review of Respiratory Disease·H Tasaka

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Citations

Jan 1, 1980·Folia Microbiologica·M Slosárek
Sep 13, 1993·Biochimica Et Biophysica Acta·E L WatsonD H Di Julio
Dec 1, 1995·FEMS Immunology and Medical Microbiology·A D DwarakanathJ M Rhodes
Oct 1, 1979·The Journal of Applied Bacteriology·J M Grange, G McIntyre
Dec 1, 1981·Tubercle·J M Grange
Mar 1, 1987·Biological Chemistry Hoppe-Seyler·J B BouwstraJ F Vliegenthart
Sep 30, 2016·World Journal of Transplantation·Darlene VigilAntonios H Tzamaloukas
Dec 1, 1985·Biotechnology Progress·A P SnyderD B Greenberg
May 1, 1984·British Journal of Industrial Medicine·E ByeC B Moncrieff
Feb 1, 1984·British Journal of Industrial Medicine·V SkaugB Gylseth
Sep 1, 1991·Microbiological Reviews·M ManafiS Bascomb

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