@article { ISI:000258200400019,
	title = {A mechanism-based ICAT strategy for comparing relative expression and activity levels of glycosidases in biological systems},
	journal = {JOURNAL OF PROTEOME RESEARCH},
	volume = {7},
	number = {8},
	year = {2008},
	month = {AUG},
	pages = {3282-3292},
	abstract = {An activity-based isotope-coded affinity tagging (AB-ICAT) strategy for proteome-wide quantitation of active retaining endoglycosidases has been developed. Two pairs of biotinylated, cleavable, AB-ICAT reagents (light H-8 and heavy D-8) have been synthesized, one incorporating a recognition element for cellulases and the other incorporating a recognition element for xylanases. The accuracy of the AB-ICAT methodology in quantifying relative glycosidase expression/activity levels in any two samples of interest has been verified using several pairs of model enzyme mixtures where one or more enzyme amounts and/or activities were varied. The methodology has been applied to the biomass-degrading secretomes of the soil bacterium, Cellulomonas fimi, under induction by different polyglycan growth substrates to obtain a quantitative profile of the relative expression/activity levels of individual active retaining endoglycanases per C. fimi cell. Such biological profiles are valuable in understanding the strategies employed by biomass-degrading organisms in exploiting environments containing different biomass polysaccharides. This is the first report on the application of an activity-based ICAT method to a biological system.},
	issn = {1535-3893},
	doi = {10.1021/pr7008302},
	author = {Hekmat, Omid and He, Shouming and Warren, R. Antony J. and Withers, Stephen G.}
}
