She, Manjunath S and Madaiah, M and Khan, MI (1988) Binding of N-dansylgalactosamine to winged-bean tuber lectin: studies by fluorescence quenching titrations. In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 954 . pp. 44-49.
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The winged-bean tuber lectin binds to N-dansyl(5-dimethylaminonaphthalene-1-sulphonic acid)galactosamine, leading to a 12.5-fold increase in dansyl fluorescence with a concomitant 25 nm blue-shift in the emission maximum. The enhancement of fluorescence intensity was completely reversed by the addition of methyl α-galactopyranoside. The lectin has two binding sites per molecule for this fluorescent sugar and an association constant of 2.59 · 105 M−1 at 25° C. The binding of N-dansylgalactosamine to the lectin shows that it can accommodate a large hydrophobic substituent on the C-2 carbon of d-galactose. Studies with other sugars indicate that a hydrophobic substituent with α-conformation at the anomeric position increases the affinity of binding. The C-4 and C-6 hydroxyl groups are also critical for sugar binding to this lectin.
|Item Type:||Journal Article|
|Additional Information:||Copy rights of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||04 Aug 2009 02:38|
|Last Modified:||19 Sep 2010 05:40|
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