• Binding site amino acid residues of jack fruit (artocarpus integrifolia) seed lectin: chemical modification and protein difference spectral studies

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    • Keywords

       

      Jack fruit seed lectin; chemical modification; difference spectra; binding site amino acids

    • Abstract

       

      The effect of chemical modification of amino acid residues essential for sugar binding in the α-D-galactoside specific jack fruit (Artocarpus integrifolia) seed lectin and the protection of the residues by specific sugar from modification were studied. Citraconylation or maleylation of 75 % of its lysyl residues or acetylation of 70 % of the tyrosyl residues completely abolished sugar binding and agglutination without dissociation of subunits. 1-O-methyl α-D-galactoside could protect its essential lysyl and tyrosyl groups from modification. Tryptophan could not be detected in the protein. Difference absorption spectra on binding of the above sugar confirmed the role of tyrosine residues and showed an association constantK = 0.4 × 103 M−1. Data suggests that the lectin could be immobilized without any loss of sugar binding activity

    • Author Affiliations

       

      P S Appukuttan1 Debkumar Basu1

      1. Neurochemistry Division, Sree Chitra Tirunal Institute for Medical Sciences and Technology, Trivandrum - 695 011, India
    • Dates

       
  • Journal of Biosciences | News

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