Interaction of Fusarium solani lectin with monosaccharides and oligosaccharides: A fluorometric study

Photochemistry and Photobiology

Volumn 83, Issue 4, 2007, Pages 966-970

  Khan, Feroz ^a   Ahmad, Absar ^a   Khan, M Islam ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

LECTIN; MONOSACCHARIDE; OLIGOSACCHARIDE;

ARTICLE; FUSARIUM; METABOLISM; SPECTROFLUOROMETRY; THERMODYNAMICS;

FUSARIUM; LECTINS; MONOSACCHARIDES; OLIGOSACCHARIDES; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

FUSARIUM SOLANI;

EID: 34447621759     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2007.00095.x     Document Type: Article

References (21)

1. Guillot, J. G. Konska (1997) Lectins in higher fungi. Biochem. Syst. Ecol. 25, 203 230.
2. Lee, Y. C. (1997) Fluorescence spectrometry in studies of carbohydrate-protein interactions. J. Biochem. (Tokyo) 121, 818 825.
3. Glaudemans, C. P. J. (1980) Methods for measuring the affinity between carbohydrate ligands and certain proteins. Methods Carbohydr. Chem. 8, 145 149.
4. Khan, F., A. Ahmad M. I. Khan (2007) Purification and characterization of a lectin from endophytic fungus Fusarium solani having complex sugar specificity. Arch. Biochem. Biophys. 457, 243 451.
5. Lis, H., N. Sharon E. Katchalski (1966) Soybean hemagglutinin a plant glycoprotein: Isolation of glycopeptide. J. Biol. Chem. 241, 684 689.
6. Townsend, R. R., M. R. Hardy, T. C. Wong Y. C. Lee (1986) Binding of N-linked bovine fetuin glycopeptides to isolated rabbit hepatocytes: Gal/GalNAc hepatic lectin discrimination between Galβ(1,4)GlcNAc and Galβ(1,3)GlcNAc in triantennary structure. Biochemistry 25, 5716 5725.
7. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248 254.
8. Dubois, M., K. K. Gills, J. K. Hamilton, P. A. Rebers F. Smoth (1956) Colorimetric method for determination of sugars and related substances. Anal. Chem. 28, 350 356.
9. Chipman, D. M., V. Grisaro N. Sharon (1967) The binding of oligosaccharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme. The specificity of binding subsites. J. Biol. Chem. 242, 4388 4394.
10. Sastry, M. V. K., P. Banarjee, R. Sankhavaram, M. Patanjali, J. Swamy, G. V. Swarnalatha A. Surolia (1986) Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal (1-3)D-GalNAc). J. Biol. Chem. 261, 11726 11733.
11. Sarkar, M., A. M. Wu E. A. Kabat (1981) Immunochemical studies on the carbohydrate specificity of Maclura pomifera lectin. Arch. Biochem. Biophys. 209, 204 218.
12. Jeyaprakash, A. A., A. Srivastava, A. Surolia M. Vijayan (2004) Structural basis for the carbohydrate specificity of Artocarpin: Variation in the length of a loop as a strategy for generating ligand specificity. J. Mol. Biol. 338, 757 760.
13. Candy, L., W. J. Peumans, L. Menu-Bouaouiche, C. H. Astoul, J. Van Damme, E. J. M. Van Damme, M. Erard M. Rougé (2001) The Gal/GalNAc specific lectin from the plant pathogenic basidiomycete Rhizoctonia solani is a member of the Ricin-B family. Biochem. Biophys. Res. Commun. 282, 655 661.
14. Candy, L., E. J. M. Van Damme, W. J. Pneumans, L. M. Bouaouiche, M. Erard P. Rouge (2003) Structural and functional characterization of the GalNAc/Gal-specific lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum (Lib.) de Bary. Biochem. Biophys. Res. Commun. 308, 396 402.
15. Gilleron, M., H. C. Siebert, H. Kaltner, C. W. von der Lieth, T. Kozar, K. M. Halkes, E. Y. Korchagina, N. V. Bovin, H. J. Gabius J. F. Vliegenthart (1998) Conformational selection and differential restriction of ligand mobility by a plant lectin - conformational behavior of Galβ1-3GlcNAcβ1-R, Galβ1-3GalNAcβ1-R and Galβ1-2β1-R′ in the free state and complexed with galactoside-specific mistletoe lectin as revealed by random-walk and conformational-clustering molecular-mechanics. Eur. J. Biochem. 252, 416 427.
16. Imberty, A., E. P. Mitchell M. Wimmerova (2005) Structural basis of high-affinity glycan recognition by bacterial and fungal lectins. Curr. Opin. Struct. Biol. 15, 525 534.
17. Kornfeld, R. S. Kornfeld (1976) Comparative aspects of glycoprotein structure. Annu. Rev. Biochem. 45, 217 238.
18. Ross, J. B. A., K. W. Rouselang L. Brand (1981) Time resolved fluorescence and anisotropy decay of the tryptophan in adrenocorticotropin-(-24) . Biochemistry 20, 4361 4369.
19. Szabo, A. G. D. M. Rayner (1980) Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102, 554 563.
20. Grinvald, A. I. Z. Steinberg (1974) On the analysis of fluorescence decay kinetics by the method of least squares. Anal. Biochem. 59, 583 598.
21. Inokuti, M. F. Hirayama (1965) Influence of energy transfer by the exchange mechanism on donor luminescence. J. Chem. Phys. 43, 1978 1989.