Binding site amino acid residues of jack fruit (Artocarpusintegrifolia) seed lectin: Chemical modification and protein difference spectral studies.
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Date
1985-03
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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-Omethyl
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 constant Κ
= 0·4 × 103 Μ-1. Data suggests that the lectin could be immobilized without any loss of sugar
binding activity.
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Keywords
Jack fruit seed lectin, chemical modification, difference spectra, binding site amino acids
Citation
Appukuttan P S, Basu Debkumar. Binding site amino acid residues of jack fruit (Artocarpusintegrifolia) seed lectin: Chemical modification and protein difference spectral studies. Journal of Biosciences. 1985 Mar; 7(1): 7-14.