Studies on Tryptophan Residues of Abrus Agglutinin. Stopped-flow Kinetics of Modification and Fluorescence-quenching Studies

Overview

Journal Biochem J

Specialty Biochemistry

Date 1987 Apr 1

PMID 3606583

Citations 2

Authors

S R Patanjali

M J Swamy

A Surolia

Affiliations

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Abstract

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

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References

Moscona A . Embryonic and neoplastic cell surfaces: availability of receptors for concanavalin A and wheat germ agglutinin. Science. 1971; 171(3974):905-7. DOI: 10.1126/science.171.3974.905. View

Davis B . DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964; 121:404-27. DOI: 10.1111/j.1749-6632.1964.tb14213.x. View

Lehrer S . Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry. 1971; 10(17):3254-63. DOI: 10.1021/bi00793a015. View

Cuatrecasas P, Tell G . Insulin-like activity of concanavalin A and wheat germ agglutinin--direct interactions with insulin receptors. Proc Natl Acad Sci U S A. 1973; 70(2):485-9. PMC: 433288. DOI: 10.1073/pnas.70.2.485. View

Lotan R, Sharon N . The fluorescence of wheat germ agglutinin and of its complexes with saccharides. Biochem Biophys Res Commun. 1973; 55(4):1340-6. DOI: 10.1016/s0006-291x(73)80041-5. View

Olsnes S, Saltvedt E, Pihl A . Isolation and comparison of galactose-binding lectins from Abrus precatorius and Ricinus communis. J Biol Chem. 1974; 249(3):803-10. View

Wei C, Koh C, PFUDERER P, Einstein J . Purification, properties, and crystallographic data for a principal nontoxic lectin from seeds of Abrus precatorius. J Biol Chem. 1975; 250(12):4790-5. View

Cermakova M, Entlicher G, KOCOUREK J . Studies on phytohemagglutinins. XXVII. A study of the pea lectin binding site. Biochim Biophys Acta. 1976; 420(2):236-45. DOI: 10.1016/0005-2795(76)90315-9. View

Privat J, Lotan R, Bouchard P, Sharon N, Monsigny M . Chemical modification of the tryptophan residues of wheat-germ agglutinin. Effect on fluorescence and saccharide-binding properties. Eur J Biochem. 1976; 68(2):563-72. DOI: 10.1111/j.1432-1033.1976.tb10844.x. View

10.

Hiromi K, Kawagishi T, Ohnishi M . Kinetic studies on the chemical modification of lysozyme by N-bromosuccinimide and its protection by substrates and analogs. J Biochem. 1977; 81(6):1583-6. DOI: 10.1093/oxfordjournals.jbchem.a131616. View

11.

Appukuttan P, Surolia A, Bachawat B . Isolation of two galactose-binding proteins from Ricinus communis by affinity chromatography. Indian J Biochem Biophys. 1977; 14(4):382-4. View

12.

Goldstein I, Hayes C . The lectins: carbohydrate-binding proteins of plants and animals. Adv Carbohydr Chem Biochem. 1978; 35:127-340. DOI: 10.1016/s0065-2318(08)60220-6. View

13.

Peterman B, LAIDLER K . The reactivity of tryptophan residues in proteins. Stopped-flow kinetics of fluorescence quenching. Biochim Biophys Acta. 1979; 577(2):314-23. DOI: 10.1016/0005-2795(79)90035-7. View

14.

Mazumder T, Gaur N, Surolia A . The physicochemical properties of the galactose-specific lectin from Momordica charantia. Eur J Biochem. 1981; 113(3):463-70. DOI: 10.1111/j.1432-1033.1981.tb05086.x. View

15.

Khan M, Surolia N, Mathew M, Balaram P, Surolia A . Fluorescence polarization as a tool to study lectin-sugar interaction. An investigation of the binding of 4-methylumbelliferyl beta-D-galactopyranoside to Abrus precatorious agglutinin. Eur J Biochem. 1981; 115(1):149-52. View

16.

Eftink M, Ghiron C . Fluorescence quenching studies with proteins. Anal Biochem. 1981; 114(2):199-227. DOI: 10.1016/0003-2697(81)90474-7. View

17.

Ashford D, Menon R, Allen A, Neuberger A . Studies on the chemical modification and potato (Solanum tuberosum) lectin and its effect on haemagglutinating activity. Biochem J. 1981; 199(2):399-408. PMC: 1163383. DOI: 10.1042/bj1990399. View

18.

Patanjali S, Swamy M, Anantharam V, Khan M, Surolia A . Chemical modification studies on Abrus agglutinin. Involvement of tryptophan residues in sugar binding. Biochem J. 1984; 217(3):773-81. PMC: 1153281. DOI: 10.1042/bj2170773. View

19.

Khan M, Sastry M, Surolia A . Thermodynamic and kinetic analysis of carbohydrate binding to the basic lectin from winged bean (Psophocarpus tetragonolobus). J Biol Chem. 1986; 261(7):3013-9. View

20.

Novogrodsky A, KATCHALSKI E . Lymphocyte transformation induced by concanavalin A and its reversion by methyl-alpha-D-mannopyranoside. Biochim Biophys Acta. 1971; 228(2):579-83. DOI: 10.1016/0005-2787(71)90064-5. View