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  • A nonradioactive 96-well plate assay for screening of trans-sialidase activity

    Author(s)
    Schrader, S
    Tiralongo, E
    Paris, G
    Yoshino, T
    Schauer, R
    Griffith University Author(s)
    Tiralongo, Evelin
    Year published
    2003
    Metadata
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    Abstract
    Trans-sialidase (E.C. 3.2.1.18) catalyzes the transfer of preferably a2,3-linked sialic acid to another glycan or glycoconjugate, forming a new a2,3 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-߭Image -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 ...
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    Trans-sialidase (E.C. 3.2.1.18) catalyzes the transfer of preferably a2,3-linked sialic acid to another glycan or glycoconjugate, forming a new a2,3 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-߭Image -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.
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    Journal Title
    Analytical Biochemistry
    Volume
    322
    DOI
    https://doi.org/10.1016/j.ab.2003.07.016
    Subject
    Analytical chemistry
    Other chemical sciences
    Biochemistry and cell biology
    Publication URI
    http://hdl.handle.net/10072/24068
    Collection
    • Journal articles

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