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4 edition of Construction and characterisation of Escherichia coli heat-labile toxin B-subunit fusion proteins found in the catalog.

Construction and characterisation of Escherichia coli heat-labile toxin B-subunit fusion proteins

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      • Thesis (Ph.D.) - University of Warwick, 1991.

        Statementtypescript
        Publisherstypescript
        Classifications
        LC Classifications1991
        The Physical Object
        Paginationxvi, 92 p. :
        Number of Pages72
        ID Numbers
        ISBN 10nodata
        Series
        1nodata
        2
        3

        nodata File Size: 4MB.


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Long-term incubation of LT or either of the mutant toxins with trypsin completely degrades the A-sub- unit data not shownbut dmLT A- subunit degradation occurs more rapidly i. De Haan L, Verweij WR, Feil IK et al 1998 Role of GM1 binding in the mucosal immunogenicity and adjuvant activity of the Escherichia coli heat-labile enterotoxin and its B subunit.

Recombinant Escherichia coli heat

90 C H A P TER 5 : T H E PARTIAL PURIFICATION O F LT-B69. The hlyA gene was found in 8 isolates. Characterization of r3CL using anti-CfaB Danti-CssA Eanti-CssB F serums, and anti-LTB G antibody. In particular, th e y are concentrated in gut- associated lymphoid tissue G A L T and bronchus-associated ly m phoid tissue B A L T. Cleavage of LT-A by trypsin into A1 21 kDa and A2 7 kDa is required for activation of the molecule and is a key factor that distinguishes native LT from mLT 8.

Construction and characterisation of heat

Streptococcus mutans and polio virus. In simple terms, the systemic response gives rise to serum antibody and effector T cells which mediate a wide range of processes: for example, opsonisation of bacteria, clearance of viral infections and transplant rejection.

However, a consistent in vitro T cell response to these epitopes could not be detected. 3 Characterisation of partially purified L T -B 6 9.