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  • 1
    Electronic Resource
    Electronic Resource
    Alteration of quaternary structure and biological activity of concanavalin A (1984)
    Springer
    The protein journal 3 (1984), S. 63-71 
    Details
    ISSN: 1573-4943
    Keywords: concanavalin A valence ; hemagglutination ; lymphocyte activation ; subunit dissociation ; tryptophan modification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A major molecular species of concanavalin A (Con A), a mitogenic lectin from jack bean seeds, has a quaternary structure composed of four homologous subunits and a tetravalent sugar-binding ability. We show that the tetrameric Con A can be converted into a monovalent monomeric form by either photochemical alkylation or hydrogen peroxide/dioxane oxidation of about two tryptophan residues. A divalent dimeric derivative of Con A is also prepared by sulfomethylamidation of about four carboxyl groups. Chemical properties and mitogenic and hemagglutinating activities of these new Con A derivates are compared with those of the tetravalent Con A, as well as of the Con A derivatives that have appeared in the literature on cell biological studies. The significance of the lectin valences in lymphocyte activation and hemagglutination is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024837
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  • 2
    Electronic Resource
    Electronic Resource
    1H NMR study of casein phosphopeptide (1-25): Assignment and conformation (1991)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 29 (1991), S. 1097-1102 
    Details
    ISSN: 0749-1581
    Keywords: 1H NMR ; Casein phosphopeptide ; 2D NMR ; COSY ; HOHAHA ; NOESY ; β-Turn ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution conformation of β-casein phosphopeptide (CPP) was studied by 1H NMR spectroscopy. As a prerequisite to the conformational analysis the spectral assignment was carried out for CPP in the Ca2+-free and -bound states by the use of two-dimensional NMR spectroscopy. The assigned resonances were used for (1) pH-titration experiments, (2) elucidation of the temperature dependence of the amide resonance and (3) a nuclear Overhauser enhancement (NOE) experiment. Although the β-turn conformation is predicted for the sequence - Val8-Pro9-Gly10-Glu11-of CPP, the present NMR results do not provide favourable evidence for its formation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260291105
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    Paper (German National Licenses)
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