Spectroscopic studies on the protective effect of a specific sugar on concanavalin A at acidic, neutral and alicaline pH

Cellular and Molecular Biology Letters

Volumn 10, Issue 1, 2005, Pages 61-72

  Khan, Rizwan Hasan ^a   Naeem, Aabgeena ^a   Baig, Masroor Alam ^b  

^a ALIGARH MUSLIM UNIVERSITY   (India)

^b HAMDARD UNIVERSITY   (India)

Author keywords

Circular Dichroism; Concanavalin A; Fluorescence; Protein Carbohydrate Interaction

Indexed keywords

ALPHA METHYLGALACTOPYRANOSIDE; ALPHA METHYLGLUCOSIDE; CONCANAVALIN A; SUGAR; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DENATURATION; FLUORESCENCE; PH; PROTEIN CARBOHYDRATE INTERACTION; SPECTROSCOPY;

EID: 17644406985     PISSN: 14258153     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Ceccatto, V.M., Cavada, B.S., Nunes, E.P., Nogueria, N.A. Grangerio, M.B., Moreno, F.B., Teixeira, E.H., Sampaio, A.H., Alves, M.A., Ramos, M.V., Calvete J.J. and Grangerio, T.B. Purification and partial characterization of a lectin from Canavalia grandiflora benth seeds. Protein Pept. Lett. 9 (2002) 67-73.
2. Loris, R., Imberty, A., Beeckmans, S., Van Driessche, E., Read, J.S., Bouckaert, J., De Greve, H., Buts, L. and Wyns, L. Crystal structure of Pterocarpus angloensis lectin in complex with glucose, sucrose and turanose. J. Biol. Chem. 33 (2003) 293-304.
3. Banerjee, R., Das, K., Ravishnjer, R., Suguna, K., Kurolia, A. and Vijayan, M. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut-lactose complex. J. Mol. Biol. 259 (1996) 281-296.
4. Sharma, V. and Surolia, A. Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J. Mol. Biol. 267 (1997) 433-445.
5. Sharon, N. and Lis, H. Lectin-proteins with a sweet tooth: function in cell recognition. Essays Biochem. 30 (1995) 59-75.
6. Lasky, L.A. Selectins: interpreters of cell-specific carbohydrate information during inflammation. Science 258 (1992) 964-969.
7. Naeem, A., Khan, R.H., Vikram, H. and Akif, M. Purification of Cajanus cajan root lectin and its interaction with Rhizobial lipopolysaccharide as studied by different spectroscopic techniques. Arch. Biochem. Biophys. 396 (2001) 99-105.
8. Auer, H.E. and Schilz, T. Denaturation of concanavalin A by urea at acid pH. Int. J. Pept. Res. 24 (1984) 569-579.
9. Sankaranarayanana, R., Sekar, K., Banarjee, R., Sharma, V., Surolia, A. and Vijayan, M. A novel mode of carbohydrate recognition in jacalin, a Moraceace plant lectin with a beta on prism fold. Nat. Struct. Biol. 3 (1996) 596-603.
10. Loris, R., Tielker, D., Jaeger, K.E. and Wyns, L. Structural basis of carbohydrate recognition by the lectin Lee B from Pseudomonas aeruginosa. J. Mol. Biol. 331 (2003) 861-870.
11. Young, N.M. and Oomen, R.P. Analysis of sequence variation among lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site. J. Mol. Biol. 228 (1992) 924-934.
12. Banerjee, R., Das, K., Ravishnjer, R., Suguna, K., Kurolia, A. and Vijayan, M. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut-lactose complex. J. Mol. Biol. 259 (1996) 281-296.
13. Sharma, V. and Surolia, A. Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J. Mol. Biol. 267 (1997) 433-445.
14. Ahmad, S., Khan, R.H. and Ahmad, A. Physicochemical characterization of Cajanus cajan lectin: effect of pH and metal ions on lectin carbohydrate interaction. Biochim. Biophys. Acta 1427 (1999) 378-384.
15. Lowry, D.H., Rosebrough, N.J., Farr, A.L. and Randal, R.J. Protein measurements with the folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275.
16. Timasheff, S.N., Sussi, H. and Stevens, L. Infrared spectra and protein conformations in aqueous solutions II. Survey of globular proteins. J. Biol. Chem. 242 (1967) 5467-5473.
17. Zand, R., Agarwal, B.B.L. and Goldstein, I.J. pH-dependent conformational changes of concanavalin A. Proc. Nat. Acad. Sci. 68 (1971) 2173-2176.
18. Datta, P.K., Basu, P.S. and Datta, T.K. Circular dichroism and fluorescence investigtaions on Vicia faba lectin-saccharide binding. IRCS Med. Sci. 12 (1984) 687-688.
19. Pere, M., Bourrillon, R. and Jirgensons, B. The use of a fluorescently labeled sugar to investigate binding by concanavalin A. Biochim. Biophys. Acta 393 (1975) 31-36.
20. Reeke, G.N., Becker, J.W. and Edelman, G.M. The covalent and three-dimensional structure of concanavalin A IV. Atomic coordinates, hydrogen quaternary structure. J. Biol. Chem. 250 (1975) 1525-547.
21. Pelley, R. and Horwitz, P. Fluorimetric studies of tryptophyl exposure in concanavalin A. Biochim. Biophys. Acta 427 (1976) 359-363.
22. Dean, B.R. and Homer, R.B. The use of a fluorescently labeled sugar to investigate binding by concanavalin A. Biochim. Biophys. Acta 322 (1973) 141-144.
23. Haq, S.K., Rasheedi, S. and Khan, R.H. Characterization of a partially folded intermediate of stem bromelain at low pH. Eur. J. Biochem. 269 (2002) 47-52.
24. Haq, S.K., Ahmad, M.F. and Khan, R.H. The acid-induced state of glucose oxidase exists as a compact folded intermediate. Biochem. Biophys. Res. Commun. 303 (2003) 685-692.
25. Naseem, F., Khan, R.H., Haq, S.K. and Naeem, A. Characterization of molten globule state of fetuin at low pH. Biochim. Biophys. Acta 1649 (2003) 164-170.
26. Khan, F., Khan, R.H. and Muzammil, S. Alcohol-induced versus anion-induced states of α-chymotrypsinogen A at low pH. Biochim. Biophys. Acta 1481 (2000) 229-236.
27. Sharon, N. Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biol. Sci. 18 (1993) 221-226.