Abstract
ElMoudni, B., Rodier, M. H., and Jacquemin, J. L. 1996. Purification and characterization ofN-acetylglucosaminidase fromTrypanosoma cruzi. Experimental Parasitology83,167–173. N-Acetyl-β-d-glucosaminidase activity was recovered in cell-free extracts ofTrypanosoma cruziepimastigotes. This enzyme was identified on the basis of its ability to hydrolyze the fluorogenic substrate 4-methylumbelliferyl-N-acetyl-β-d-glucosaminide. This activity was purified to apparent homogeneity by anion exchange and molecular sieve high-performance liquid chromatography. It eluted at a native molecular weight of approximatlly 48,000 Da and migrated as a single band upon reducing or nonreducing sodium dodecyl sulfate–polyacrylamide gel electrophoresis. The optimum pH of the activity was around pH 5.4 and the enzyme gave a single peak of activity on a chromatofocusing column with an isoelectric point of 4.2. The enzyme hydrolyzed 4-methylumbelliferyl-GlcNAc, suggesting that it should be characterized as aN-acetyl-β-dglucosaminidase, with aKmvalue of 1.5 mMfrom Lineweaver-Burk plots. Many inhibitors as potential enzyme effectors were investigated.
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