Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
1997 | 44 | 2 |
Tytuł artykułu

The N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves

Treść / Zawartość
Warianty tytułu
Języki publikacji
The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.
Opis fizyczny
  • University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland
  • 1. Peumans, W.J. & Stinissen, H.M. (1983) Gramineae lectins: Occurrence, molecular bi­ology and physiological function; in Chemical Taxonomy, Molecular Biology and Function of Plant Lectins (Goldstein, I.J. & Etzler, M.E., eds.) pp. 99 116, A.R.Lis Inc., New York.
  • 2. Stinissen, H.M., Peumans, W.J. & Carlier, A.R. (1983) Occurrence and immunological relationships of lectins in gramineous species. Planta 159, 105-111.
  • 3. Mo, H., Van Damme, E.J.M., Peumans, W.J. & Goldstein, I.J. (1993) Purification and char­acterization of a mannose specific lectin from shallot (Allium ascalonicum). Arch. Biochem. Biophys. 306, 431-438.
  • 4. Van Damme, E.J.M., Smeets, K., Engel- borghs, I., Aelbers, H., Balzarini, J., Pustai, A., Van Leuven, F., Goldstein, I.J. & Peu­mans, W.J. (1993) Cloning and charac­terization of the lectin cDNA clones from on­ion, shallot and leek. Plant Mol. Biol. 23, 365-376.
  • 5. Cammue, B.P.A., Peeters, B. & Peumans, W.J. (1986) A new lectin from tulip (Tulipa) bulbs. Planta 169, 583-588.
  • 6. Van Damme, E.J.M., Allen, A.K. & Peumans, W.J. (1987) Isolation and characterization of a lectin with exclusive specificity towards mannose from snowdrop (Gallanthus nivalis) bulbs. FEBS Lett. 215, 140-144.
  • 7. Van Damme, E.J.M., Allen, A.K. & Peumans, W.J. (1988) Related mannose-specific lectins from different species of the family Amaryli- daceae. Physiol. Plant. 73, 52-57.
  • 8. Van Damme, E.J.M., Goldstein, I.J., Vercam- men, G., Vuylsteke, J. & Peumans, W.J. (1992) Lectins of members of Amarylidaceae are encoded by multigene families which show extensive homology. Physiol. Plant. 86, 245-252.
  • 9. Saito, K., Komae, A., Kakuta, M., Van Damme, E.J.M., Peumans, W.J., Goldstein, I. J. & Misaki, A. (1993) The a-mannosyl-bind- ing lectin from leaves of the orchid twayblade (Listera ouata). Application to separation of cc-D-mannans from a-D-glucans. Eur. J. Bio­chem. 217, 677-681.
  • 10. Goldstein, I.J. & Hayes, C.E. (1978) The lect­ins. Adv. Carbohydr. Chem. Biochem. 35. 127-340.
  • 11. Van Damme, E.J.M., Goldstein, I.J. & Peu­mans, W.J. (1991) Comparative study of re­lated mannose-binding lectins from Amaryllt- daceae and Alliaceae species. Phytochemistry 30, 509-514.
  • 12. Ferens-Sieczkowska, M. & Morawiecka, B. (1993) GalNAc/Gal specific lectin from ger- man iris (Iris germanica). Acta Biochim. Polon. 40, 123-124.
  • 13. Van Damme, E.J.M. & Peumans, W.J. (1989) Developmental changes and tissue distribu­tion of lectin in Tulipa. Planta 178, 10-18.
  • 14. Van Damme, E.J.M. & Peumans, W.J. (1990) Developmental changes and tissue distribu­tion of lectin in Galanthus nivalis L. and Narcissus cv. Carlton. Planta 182, 605 609.
  • 15. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
  • 16. Smith, P.K., Krohn, R.I. & Hermanson, G.T. (1985) Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
  • 17. Dubois, M., Gilles, K.A., Hamilton, J.K., Re- bevs, P.A. & Smith, F. (1956) Colorimetric method for determination of sugar and re­lated substances. Anal. Chem. 28, 350-356.
  • 18. Duk, M., Lisowska, E., Wu, J.H. & Wu, A.M. (1994) The biotin/avidin mediated microtiter plate lectin assay with the use of chemically modified glycoprotein ligand. Anal. Biochem. 221, 266-272.
  • 19. Lacmmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
  • 20. Merril, C.R., Goldman, D., Sedman, S.A. & Ebert, M.H. (1981) Ultrasensitive stain for proteins in polyacrylamide gels shows vari­ation in cerebrospinal fluid proteins. Science 211, 1437-1438.
  • 21. Conrad, F. & Rüdiger, H. (1994) The lectin from Pleurotus ostrealus: Purification, char­acterization, and interaction with a phos­phatase. Phytochemistry 36, 277-288.
  • 22. Ahmed, H., Ray, S. & Chatteije, B.P. (1988) A low molecular weight agglutinin from Ficus carica. 10th International Lectin Conference, Abstracts, p. 15, Prague, 03-08, July, 1988.
  • 23. Ray, S., Chatteije, B.P. & Ahmed, H. (1988) pH-dependent agglutinin from Ficus ben- galensis. 10th International Lectin Confer­ence, Abstracts, p. 65, Prague, 03-08, July, 1988.
  • 24. Shibuya, N., Goldstein, I.J., Van Damme, E.J.M. & Peumans, W.J. (1988) Binding prop­erties of a mannose-spccific lcctin from the snowdrop (Galanthus nivalis) bulb. J. Biol. Chem. 263, 728-734.
  • 25. Peumans, W.J., Allen, A.K. & Cammue, B.P.A. (1986) A new lectin from meadow saf­fron (Colchicum autumnale). Plant Physiol. 82, 1036-1040.
  • 26. Lis, H., Joubert, F.J. & Sharon, N. (1985) Isolation and properties of N-acetyllac- tosamine-specific lectins from nine Erythrina species. Phytochemistry 24, 2803-2809.
  • 27. Togun, R.A., Animashaun, T., Kay, J.E. & Aboderin, A.A. (1994) A galactose binding T-cell mitogenic lectin from the seeds of Telfairia occidentalis. Phytochemistry 35, 1125-1130.
  • 28. Sastry, M.V.K., Banaijee, P., Patanjali, S.R., Swamy, M.J., Swarnalatha, G.V. & Surolia, A. (1986) Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (p-D-Gal(l-»3)D-Gal- NAc).J. Biol. Chem. 261, 11726-11733.
Typ dokumentu
Identyfikator YADDA
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.