1887

Abstract

Purified preparations of the extracellular glucan of and the walls of were shown to contain enzymically active protein. The glucans and walls were treated in various ways to liberate the protein and determine the nature and strength of its binding, if any, to each matrix. Binding of protein to the glucan appeared to be non-covalent and was specific only in that the native protein seemed to bind more firmly than protein derived from other fungal genera. Binding of protein to walls appeared to be stronger than to the glucan but in each case protein was found to be less stable when freed from its carbohydrate matrix. Protein liberated from glucan showed enhanced activity although its remained the same; thus, this matrix acted in the same manner as a non-competitive inhibitor. Protein liberated from walls was less active than when attached. The differences between the two matrices, with respect to protein binding, are discussed in the light of possible differences in their tertiary structure.

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1979-05-01
2024-04-16
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References

  1. Anderson A. J. 1978; Isolation from three species of Coiletotrichum of glucan-containing polysaccharides that elicit browning and phytoalexin production in bean. Phytopathology 68:189–194
    [Google Scholar]
  2. Anderson–Prouty A. J., Albersheim P. 1975; Host–pathogen interactions. VIII. Isolation of a pathogen-synthesized fraction rich in glucan that elicits a defense response in the pathogen′s host. Plant Physiology 56:286–291
    [Google Scholar]
  3. Atkins E. D. T.,, Parker K. D., Preston R. D. 1969; The helical structure of the β-1,3-linked xylan in some siphoneous green algae. Proceedings of the Royal Society B173:209–221
    [Google Scholar]
  4. Ayers A. R., Ebel J., Finelli F., Berger N., Albersheim P. 1976a; Host–pathogen interactions. IX. Quantitative assays of elicitor activity and characterization of the elicitor present in the extracellular medium of cultures of Phytophthora megasperma var. sojae. Plant Physiology 57:751–759
    [Google Scholar]
  5. Ayers A. R., Ebel J., Valent B., Albersheim P. 1976a; Host–pathogen interactions. X. Fractionation and biological activity of an elicitor isolated from the mycelial walls of Phytophthora megasperma var. sojae. . Plant Physiology 57:760–765
    [Google Scholar]
  6. Ayers A. R., Valent B., Ebel J., Albersheim P. 1976c; Host–pathogen interactions. XI. Composition and structure of wall-released elicitor fractions. Plant Physiology 57:766–774
    [Google Scholar]
  7. Bartnicki-Garcia S. 1970; Cell wall composition and other biochemical markers in fungal phylogeny. In Phytochemical Phylogeny pp. 81–103 Edited by Harborne J. B. London and New York :: Academic Press.;
    [Google Scholar]
  8. Bartnicki-Garcia S. 1973; Fungal cell wall composition. In Handbook of Microbiology vol. II, pp. 201–214 Edited by Laskin A. I., Cleveland H. A. Lechevalier. Ohio :: CRC Press;
    [Google Scholar]
  9. Brandenberger H., Henson R. 1953; Eine spektrophotometrische Bestimmungsmethode für saure und alkalische Phosphatasen. Helvetica chimica acta 36:900–906
    [Google Scholar]
  10. Buck K. W., Chen A. W., Dickerson A. G., Chain E. B. 1968; Formation and structure of extracellular glucans produced by Claviceps species. Journal of General Microbiology 51:337–352
    [Google Scholar]
  11. Burrows W. 1963; In Textbook of Microbiology,. , 18th edn.p. 50. Edited by Burrows W. Philadelphia:: W. B. Saunders;
    [Google Scholar]
  12. Clarke A. E., Stone B. A. 1963; Chemistry and biochemistry of β-1,3-glucans. Review of Pure and Applied Chemistry 13:134–156
    [Google Scholar]
  13. Clarke A. E., Stone B. A. 1965; β-Glucan hydrolases from Aspergillus niger: isolation of a β-(1→4)-glucan hydrolase and some properties of the β-(1→3)-glucan-hydrolase components. Biochemical Journal 96:793–801
    [Google Scholar]
  14. Chrambach A., Reisfeld R. A., Wyckoff M., Zaccari J. 1967; A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis. Analytical Biochemistry 20:150–154
    [Google Scholar]
  15. Dickerson A. G. 1972; A β-D-fructofuranosidase from Claviceps purpurea. Biochemical Journal 129:263–272
    [Google Scholar]
  16. Dickerson A. G., Mantle P. G., Szczyrbak C. A. 1970; Autolysis of extracellular glucans produced in vitro by a strain of Claviceps fusi-formis. Journal of General Microbiology 60:403–415
    [Google Scholar]
  17. Dickerson A. G., Mantle P. G., Nisbet L. J. 1976; Carbon assimilation by Claviceps purpurea growing as a parasite. Journal of General Microbiology 97:267–276
    [Google Scholar]
  18. Dubois M., Gilles K. A., Hamilton J. K., Rebers P. A., Smith F. 1951; A colorimetric method for the determination of sugars. Nature, London168–167
    [Google Scholar]
  19. Dubois M., Gilles K. A., Hamilton J. K., Rebers P. A., Smith F. 1956; A colorimetric method for the determination of sugars and related substances. Analytical Chemistry 28:350–356
    [Google Scholar]
  20. Ebel J., Ayers A. R., Albersheim P. 1976; Host–pathogen interactions XII. Response of suspension-cultured soybean cells to the elicitor isolated from Phytophthora megasperma var. sojae, a fungal pathogen of soybeans. Plant Physiology 57:775–779
    [Google Scholar]
  21. Fairbanks G., Steck T. L., Wallach D. F. H. 1971; Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617
    [Google Scholar]
  22. Fennell T. R. W. F.,, Roberts M. W., Webb J. R. 1957; The semi-micro determination of phosphorus in fluorinated organic compounds. Analyst 82:639–643
    [Google Scholar]
  23. Fèvre, M. 1977; Subcellular localization of glucanase and cellulase in Saprolegnia monoica Pringsheim. Journal of General Microbiology 103:287–295
    [Google Scholar]
  24. Fleet G. H., Manners D. J. 1976; Isolation and composition of an alkali-soluble glucan from the cell walls of Saccharomyces cerevisiae. Journal of General Microbiology 94:180–192
    [Google Scholar]
  25. Fleet G. H., Manners D. J. 1977; The enzymic degradation of an alkali-soluble glucan from the cell walls of Saccharomyces cerevisiae. Journal of General Microbiology 98:315–327
    [Google Scholar]
  26. Fleet G. H., Phaff H . J. 1974; Glucanases in Schizosaccharomyces. Isolation and properties of the cell wall-associated β-(1→3)-glucanases. Journal of Biological Chemistry 249:1717–1728
    [Google Scholar]
  27. Gabriel O., Wang S. F. 1969; Determination of enzymatic activity in polyacrylamide gels. Analytical Biochemistry 27:545–554
    [Google Scholar]
  28. Garza A. C., Weissler H. E. 1967; Automatic simultaneous multiple chemical analyses of worts and beers. Technicon Symposium 1:201–206
    [Google Scholar]
  29. Keen N. T. 1975; Specific elicitors of plant phytoalexin production: determinants of race specificity in pathogens?. Science 187:74–75
    [Google Scholar]
  30. Keen N. T., Wang M. C., Bartnicki-Garcia S., Zentmyer G. A. 1975; Phytotoxicity of mycolaminarins – β-1,3-glucans from Phytophthora spp. Physiological Plant Pathology 7:91–97
    [Google Scholar]
  31. Kritzman G., Chet I., Henis Y. 1978; Localization of β-1,3-glucanase in the mycelium of Sclerotium rolfsii.. Journal of Bacteriology 134:470–475
    [Google Scholar]
  32. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  33. Mantle P. G. 1968; Studies of Sphacelia sorghi McRae, an ergot of Sorghum vulgare Pers. Annals of Applied Biology 62:443–449
    [Google Scholar]
  34. Mantle P. G., Waight E. S. 1968; Dihydro-ergosine: a new naturally occurring alkaloid from the sclerotia of Sphacelia sorghi McRae. Nature, London 218:581–582
    [Google Scholar]
  35. Moorhouse R., Winter W. T., Arnott S., Bayer M. E. 1977; Conformation and molecular organization in fibers of the capsular polysaccharide from Escherichia coli M41 mutant. Journal of Molecular Biology 109:373–391
    [Google Scholar]
  36. Morris D. L. 1948; Quantitative determination of carbohydrates with Dreywood′s anthrone reagent. Science 107:254–255
    [Google Scholar]
  37. Morris E. R., Rees D. A., Young G., Walkinshaw M. D., Darke A. 1977; Order–disorder transition for a bacterial polysaccharide in solution. A role for polysaccharide conformation in recognition between Xanthomonas pathogen and its plant host. Journal of Molecular Biology 110:1–16
    [Google Scholar]
  38. Mower R. L., Gray G. R., Ballou C. E. 1973; Sugars from Sphacelia sorghi honeydew. Carbohydrate Research 27:119–134
    [Google Scholar]
  39. Perlin A. S., Taber W. A. 1963; A glucan produced by Claviceps purpurea.. Canadian Journal of Chemistry 41:2278–2282
    [Google Scholar]
  40. Rees D. A. 1973; Polysaccharide conformation. In MTP International Review of Science: Carbohydrates. Organic Chemistry, Series 1 vol. 7251–283 Edited by Aspinall G. O. London:: Butterworths.;
    [Google Scholar]
  41. Reese E. T., Mandels M. 1966; β-Glucanases other than cellulase. Methods in Enzymology 8:607–615
    [Google Scholar]
  42. Sietsma J. H., Wessels J. G. H. 1977; Chemical analysis of the hyphal wall of Schizophyllum commune. Biochimica et biophysica acta 496:225–239
    [Google Scholar]
  43. Stekoll M., West C. A. 1978; Purification and properties of an elicitor of castor bean phytoalexin from culture filtrates of the fungus Rhizopus stolonifer. Plant Physiology 61:38–45
    [Google Scholar]
  44. Villa T., G ., Notario V., Villanueva J. R. 1976; Method of purifying β-(1→3)-glucanase from Candida utilis. Applied and Environmental Microbiology 32:185–187
    [Google Scholar]
  45. Villanueva J. R., Notario V., Santos T., Villa T. G. 1976; β-Glucanases in nature: bio-chemistry and function of β-glucanases in yeast. In Microbiology and Plant Protoplasts pp. 323–355 Edited by Peberdy J. F., Rose A. H., Rogers H. J., Cocking E. C. London and New York:: Academic Press.;
    [Google Scholar]
  46. Weber K., Pringle J. R., Osborn M. 1972; Measurements of molecular weights by electrophoresis on acrylamide gels. Methods in Enzymology 26C:3–27
    [Google Scholar]
  47. Wessels J. G. H.,, Kreger D. R., Marchant R., Regensburg B. A., De Vries O. H. M. 1972; Chemical and morphological characterization of the hyphal wall surface of the basidiomycete Schizophyllum commune. Biochimica et biophysica acta 273:346–358
    [Google Scholar]
  48. Whistler R. L., Bushway A. A., Singh P. P., Nakahara W., Tokuzen R. 1976; Noncyto-toxic, antitumor polysaccharides. Advances in Carbohydrate Chemistry and Biochemistry 32:235–275
    [Google Scholar]
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