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• W2072542559 abstract "Trans-sialidase (E.C. 3.2.1.18) catalyzes the transfer of preferably alpha2,3-linked sialic acid to another glycan or glycoconjugate, forming a new alpha2,3 linkage to galactose or N-acetylgalactosamine. Here, we describe a nonradioactive 96-well plate fluorescence test for monitoring trans-sialidase activity with high sensitivity, specificity, and reproducibility using sialyllactose and 4-methylumbelliferyl-beta-D-galactoside as donor and acceptor substrates, respectively. The assay conditions were optimized using the trans-sialidase from Trypanosoma congolense and its general applicability was confirmed with recombinant trans-sialidase from Trypanosoma cruzi. Using this procedure, a large number of samples can be tested quickly and reliably, for instance in monitoring trans-sialidase during enzyme purification and the production of monoclonal antibodies, for enzyme characterization, and for identifying potential substrates and inhibitors. The trans-sialidase assay reported here was capable of detecting trans-sialidase activity in the low-mU range and may be a valuable tool in the search for further trans-sialidases in various biological systems." @default.
• W2072542559 created "2016-06-24" @default.
• W2072542559 creator A5050298434 @default.
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• W2072542559 date "2003-11-01" @default.
• W2072542559 modified "2023-09-23" @default.
• W2072542559 title "A nonradioactive 96-well plate assay for screening of trans-sialidase activity" @default.
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• W2072542559 doi "https://doi.org/10.1016/j.ab.2003.07.016" @default.
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