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Updated: Aug 7, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 27, 2011
Studies on recombinant single chain Jacalin lectin reveal reduced affinity for saccharides despite normal folding
Anagh A Sahasrabuddhe1, Sushama M Gaikwad, M V Krishnasastry
1National Centre for Cell Science, Pune, Maharashtra, India.
Abstract:
Sugar binding studies, inactivation, unfolding, and refolding of native Jacalin (nJacalin) from Artocarpus integrifolia and recombinant single-chain Jacalin (rJacalin) expressed in Escherichia coli were studied by intrinsic fluorescence and thermal and chemical denaturation approaches. Interestingly, rJacalin does not undergo any proteolytic processing in an E. coli environment. It has 100fold less affinity for methyl-alpha-galactose (Ka: 2.48 x 10(2)) in comparison to nJacalin (Ka: 1.58 x 10(4)), and it also binds Thomsen-Friedenreich (TF) disaccharide (Galbeta1-3GalNAc) with less affinity. Overall sugar binding characteristics of rJacalin are qualitatively similar to that of nJacalin (Gal
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