Differential scanning calorimetric studies of the glycoprotein, winged bean acidic lectin, isolated from the seeds of Psophocarpus tetrogonolobus

FEBS Letters
V R SrinivasA Surolia

Abstract

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 WBAII 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.

References

Jul 16, 1985·Biochemistry·S P ManlyJ M Sturtevant
Jul 26, 1996·The Journal of Biological Chemistry·A SuroliaF P Schwarz

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Citations

Jul 26, 2015·International Journal of Biological Macromolecules·Mazen Haj SleimanMaria Micha-Screttas
Feb 16, 1999·FEBS Letters·M J MarcosV L Shnyrov
Oct 22, 2004·The Biochemical Journal·Ricardo FrancoMargarida Bastos
May 17, 2017·Biophysics Reviews·Natalia A ChebotarevaBoris I Kurganov
Jul 5, 2017·The Biochemical Journal·Nisha Grandhi Jayaprakash, Avadhesha Surolia
Aug 31, 2019·Progress in Biophysics and Molecular Biology·L Alaei, Ali A Moosavi-Movahedi
Apr 12, 2006·Biochemistry·Rasmus Høiberg-NielsenPeter Westh
Jul 17, 1999·Analytical Chemistry·C K LariveS Bogdanowich-Knipp

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