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Studies on recombinant single chain Jacalin lectin reveal reduced affinity for saccharides despite normal folding like native Jacalin
Author(s) -
Sahasrabuddhe Anagh A.,
Gaikwad Sushama M.,
Krishnasastry M.V.,
Khan M. Islam
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04968804
Subject(s) - jacalin , chemistry , lectin , denaturation (fissile materials) , biochemistry , recombinant dna , circular dichroism , biophysics , biology , nuclear chemistry , gene
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‐α‐galactose (Ka: 2.48 × 10 2 ) in comparison to nJacalin (Ka: 1.58 × 10 4 ), and it also binds Thomsen‐Friedenreich (TF) disaccharide (Galβ1–3GalNAc) with less affinity. Overall sugar binding characteristics of rJacalin are qualitatively similar to that of nJacalin (Gal