Characterisation of immune proteins from Clarias sp. and Pangasius sp

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Aquaculture was introduced in the Sub-Sahara as an innovation to improve economies and nutrition of local communities. After years of local and international investment, aquaculture is still struggling with basic issues such as limited personnel, poor training in aquaculture technologies and practice, lack of appropriate aquaculture species and diseases. This book sets out to describe the methodology of isolating and characterising immune proteins (lectins and immunoglobulin mu (IgM)) from the African cat fish, Clarias gariepinus and Pangasius hypophthalmus which is a basis for developing tools for monitoring fish health. More than one affinity chromatography isolation steps are required to isolate Serum Amyloid Protein, C-reactive protein, mannose and galactose binding proteins. The purified fractions migrate as more than one band in Tris-tricine SDS-PAGE in the presence of beta-mercaptoethanol. On the other hand IgM isolated from P. hypophthalmus seem to use a single recognition site to bind to fucose and GlcNAc. The implication of these findings can not be ignored when considering using these sugar binding lectins and IgM as tools for monitoring fish health.

Autorentext

Thomson studied Biology at University of Malawi before proceeding to master molecular biology and biotechnology at Katholieke Univesitiet Leuven in Belgium. Currently pursuing a PhD topic in molecular genetics at Stellenbosch University in South Africa. Thomson is a faculty at the Lilongwe University of Agriculture and Natural Resources in Malawi

Weitere Informationen

  • Allgemeine Informationen
    • GTIN 09783330011984
    • Sprache Englisch
    • Genre Biology
    • Größe H220mm x B150mm
    • Jahr 2016
    • EAN 9783330011984
    • Format Kartonierter Einband
    • ISBN 978-3-330-01198-4
    • Titel Characterisation of immune proteins from Clarias sp. and Pangasius sp
    • Autor Thomson Sanudi , Sonia Beckmanns
    • Herausgeber LAP Lambert Academic Publishing
    • Anzahl Seiten 108

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