Abstract
This work provides evidence of a physical instance in which some proteins that are usually inactivated under strong chaotropic conditions may become fully resistant through the occupancy of their binding sites with suitable ligands. In this regard, we found that Moluccella laevis lectin remains stable in the presence of denaturant concentrations of urea when an appropriate saccharide is bound to the protein (Alperin, D. M., Latter, H., Lis, H., and Sharon, N. (1992) Biochem. J. 285, 1-4). Extending this finding, we now demonstrate that the occupancy of the ligand binding sites of concanavalin A (Con A) with appropriate carbohydrates completely prevents the denaturation course elicited by 8 M urea at pH 7.4. In addition, the protecting efficiency of the saccharides was shown to be directly related to their specificities for the lectin. The observed saccharide protection follows the order: methyl α-D-mannopyranoside > methyl α-D-glucopyranoside > mannose > fructose > glucose. Concomitantly, the active tetrameric lectin with a molecular mass of ~105 kDa is preserved in 8 M urea when methyl α- D-mannopyranoside (100 mM) is present in the medium.
| Original language | English |
|---|---|
| Pages (from-to) | 154-158 |
| Number of pages | 5 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 340 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1 Apr 1997 |
| Externally published | Yes |
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Keywords
- chaotropic effect
- chaotropic effect suppression
- concanavalin A
- lectin
- protein unfolding
- protein unfolding protection
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Dramatic saccharide-mediated protection of chaotropic-induced deactivation of concanavalin A. / Figlas, Débora N.; Arias, Hugo R.; Fernández, Ariel; Alperin, Daniel M.
In: Archives of Biochemistry and Biophysics, Vol. 340, No. 1, 01.04.1997, p. 154-158.Research output: Contribution to journal › Article
TY - JOUR
T1 - Dramatic saccharide-mediated protection of chaotropic-induced deactivation of concanavalin A
AU - Figlas, Débora N.
AU - Arias, Hugo R.
AU - Fernández, Ariel
AU - Alperin, Daniel M.
PY - 1997/4/1
Y1 - 1997/4/1
N2 - This work provides evidence of a physical instance in which some proteins that are usually inactivated under strong chaotropic conditions may become fully resistant through the occupancy of their binding sites with suitable ligands. In this regard, we found that Moluccella laevis lectin remains stable in the presence of denaturant concentrations of urea when an appropriate saccharide is bound to the protein (Alperin, D. M., Latter, H., Lis, H., and Sharon, N. (1992) Biochem. J. 285, 1-4). Extending this finding, we now demonstrate that the occupancy of the ligand binding sites of concanavalin A (Con A) with appropriate carbohydrates completely prevents the denaturation course elicited by 8 M urea at pH 7.4. In addition, the protecting efficiency of the saccharides was shown to be directly related to their specificities for the lectin. The observed saccharide protection follows the order: methyl α-D-mannopyranoside > methyl α-D-glucopyranoside > mannose > fructose > glucose. Concomitantly, the active tetrameric lectin with a molecular mass of ~105 kDa is preserved in 8 M urea when methyl α- D-mannopyranoside (100 mM) is present in the medium.
AB - This work provides evidence of a physical instance in which some proteins that are usually inactivated under strong chaotropic conditions may become fully resistant through the occupancy of their binding sites with suitable ligands. In this regard, we found that Moluccella laevis lectin remains stable in the presence of denaturant concentrations of urea when an appropriate saccharide is bound to the protein (Alperin, D. M., Latter, H., Lis, H., and Sharon, N. (1992) Biochem. J. 285, 1-4). Extending this finding, we now demonstrate that the occupancy of the ligand binding sites of concanavalin A (Con A) with appropriate carbohydrates completely prevents the denaturation course elicited by 8 M urea at pH 7.4. In addition, the protecting efficiency of the saccharides was shown to be directly related to their specificities for the lectin. The observed saccharide protection follows the order: methyl α-D-mannopyranoside > methyl α-D-glucopyranoside > mannose > fructose > glucose. Concomitantly, the active tetrameric lectin with a molecular mass of ~105 kDa is preserved in 8 M urea when methyl α- D-mannopyranoside (100 mM) is present in the medium.
KW - chaotropic effect
KW - chaotropic effect suppression
KW - concanavalin A
KW - lectin
KW - protein unfolding
KW - protein unfolding protection
UR - http://www.scopus.com/inward/record.url?scp=0031127717&partnerID=8YFLogxK
U2 - 10.1006/abbi.1997.9929
DO - 10.1006/abbi.1997.9929
M3 - Article
C2 - 9126288
AN - SCOPUS:0031127717
VL - 340
SP - 154
EP - 158
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -