BINDING-SITE AMINO-ACID RESIDUES OF JACK FRUIT (ARTOCARPUS-INTEGRIFOLIA) SEED LECTIN - CHEMICAL MODIFICATION AND PROTEIN DIFFERENCE SPECTRAL STUDIES

The effect of chemical modification of amino acid residues essential for sugar binding in the .alpha.-D-galactoside specific jack fruit (A. 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-.alpha.-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 constant K = 0.4 .times. 103 M-1. The lectin could be immobilized without any loss of sugar binding activity.