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Journal of Biosciences

, Volume 7, Issue 1, pp 7–14 | Cite as

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

  • P. S. Appukuttan
  • Debkumar Basu
Article

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

Keywords

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

Abbreviations used

JSA

Jack fruit seed agglutinin

methyl α-gal

1-O-methyl α-D-galactopyranoside

methyl α-glc

1-O-methyl α-D-glucopyranoside

TNBS

trinitrobenzene sulphonate

PBS

20 mM phosphate buffer with 150 mM NaCl, pH 7.4

SDS

sodium dodecyl sulphate

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Copyright information

© Indian Academy of Sciences 1985

Authors and Affiliations

  • P. S. Appukuttan
    • 1
  • Debkumar Basu
    • 1
  1. 1.Neurochemistry DivisionSree Chitra Tirunal Institute for Medical Sciences and TechnologyTrivandrumIndia

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