Srinivas, VR and Singha, Netai C and Schwarz, Fredrick P and Surolia, Avadhesa (1998) Differential scanning calorimetric studies of the glycoprotein, winged bean acidic lectin, isolated from the seeds of Psophocarpus tetrogonolobus. In: FEBS Letters, 425 (1). pp. 57-60.
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Differential scanning calorimetry of solutions of WBAII and in presence of sugar ligands shows that WBAII dimer dissociates to its constituent monomeric subunits at the denaturation temperature, The thermal denaturation of WB;UI consists of the unfolding of two independent domains of WBAII similar to that of basic winged bean lectin and ECorL and in contrast to concanavalin A (conA), pea and lentil lectin, which unfold as single entities. Apparently, the glycosylation reduces the structural integrity of WBAII as compared to conA, pea and lentil Lectin, The increase in the denaturation temperature of the sugar-lectin complexes yields binding constants close to the binding constants extrapolated from the ITC results and confirms the mechanism proposed for its thermal unfolding.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Keywords:||scanning calorimetry;WBAII;quaternary association; denaturation temperature.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||18 May 2009 05:50|
|Last Modified:||19 Sep 2010 05:01|
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