Generation of Lectins from Enzymes: Use of Inactive Endosialidase for Polysialic Acid Detection

Anne Jokilammi*, Miikka Korja, Elina Jakobsson, Jukka Finne

*Corresponding author for this work

    Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

    Abstract

    Enzyme-substrate interactions are comparable to lectin-carbohydrate or antigen-antibody interactions in terms of specificity. The dissociation constant (KD) values of lectins and enzymes are comparable (generally from millimolar to micromolar). Despite the enormous potential of specific interactions, enzyme-substrate interactions have generally not been exploited as a source for the construction of specific molecular probes, such as lectins. Polysialic acid (polySia) is a developmentally regulated carbohydrate polymer involved in neural cell differentiation, organogenesis, and malignancies. PolySia represents an important developmental antigen, and its specific detection method could be utilized to study neural plasticity, various malignancies, and central nervous system infections. Inactivated endosialidase represents a new approach to detect polySia, which due to the poor immunogenicity has been a complicated target for the production of antibodies. This chapter describes a catalytically inactive bacteriophage-derived endosialidase that can be used as a probe with lectin-like properties in the specific detection of its substrate, polySia.

    Original languageEnglish
    Title of host publicationLectins: Analytical Technologies
    PublisherElsevier
    Pages385-395
    Number of pages11
    ISBN (Print)9780444530776
    DOIs
    Publication statusPublished - 2007

    Fingerprint Dive into the research topics of 'Generation of Lectins from Enzymes: Use of Inactive Endosialidase for Polysialic Acid Detection'. Together they form a unique fingerprint.

    Cite this