Proceedings of the National Academy of Sciences · 1994 · 177 citations · 13 references
Life SciencesBiochemistryMicrobiologyCarbohydrate BiochemistryEnzymologyMicrobial MetabolismBacterial MetabolismCarbohydrate StructureCellulose BiochemistryMacromolecular InteractionsCellulase ActivityCellulase BiologyCellulase EnzymesCellulose HydrolysisFibers
Endoglucanase A (CenA) from the bacterium Cellulomonas fimi is composed of a catalytic domain and a nonhydrolytic cellulose-binding domain that can function independently. The individual domains interact synergistically in the disruption and hydrolysis of cellulose fibers. This intramolecular synergism is distinct from the well-known intermolecular synergism between individual cellulases. The catalytic domain corresponds to the hydrolytic Cx system and the cellulose-binding domain corresponds to the nonhydrolytic C1 system postulated by Reese et al. [Reese, E. T., Sui, R. G. H. & Levinson, H. S. (1950) J. Bacteriol. 59, 485-497] to be required for the hydrolysis of cellulose.
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Measurement of protein by spectrophotometry at 205 nm
R.K. Scopes · Analytical Biochemistry · 1974 · 764 citations
Neil R. Gilkes, R. A. J. Warren, Robert C. Miller et al. · Journal of Biological Chemistry · 1988 · 346 citations · Full text