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Properties of protein constituents of black locust bark

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Summary

The total protein content of black locust bark increased in December, remained at an elevated level throughout the winter and spring, and decreased in June. Hemagglutinating activity of lectin in the bark did not follow this pattern but increased to a maximum in February and decreased in March. Lectin may be involved in protein storage as others have suggested, but the role of its ability to bind carbohydrates is not evident. A role for lectin as a protective compound could not be assigned because lectin extracts did not inhibit bacterial or fungal growth even though they affected fungal growth characteristics. Chitinase activity, however, was present in black locust inner bark at a concentration which inhibited fungal growth in vitro.

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References

  • Abeles, F. B.; Bosshart, R. P.; Forrence, L. E.; Habig, W. H. 1970: Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol. 47: 129–134

    Google Scholar 

  • Bolwell, G. P. 1987: Elicitor induction of the synthesis of a novel lectin-like arabinosylated hydroxyproline-rich glycoprotein in suspension cultures of Phaseolus vulgaris L. Planta 172: 184–191

    Google Scholar 

  • Fink, W.; Liefland, M.; Mendgen, K. 1988: Chitinases and β-1,3-glucanases in the apoplastic compartment of oat leaves (Avena sativa L.). Plant Physiol. 88: 270–275

    Google Scholar 

  • Gietl, C.; Ziegler, H. 1980: Distribution of carbohydrate-binding proteins in different tissues of Robinia pseudoacacia L. Biochem. Physiol. Pflanzen 175: 58–66

    Google Scholar 

  • Hackman, R. H.; Goldberg, M. 1964: New substrates for use with chitinases. Anal. Biochem. 8: 397–401

    Google Scholar 

  • Hankins, C. N.; Kindinger, J.; Shannon, L. M. 1987: The lectins of Sophora japonica I. Purification, properties, and N-terminal amino acid sequences of two lectins from leaves. Plant Physiol. 83: 825–829

    Google Scholar 

  • Hankins, C. N.; Kindinger, J. I.; Shannon, L. M. 1988: The lectins of Sophora japonica II. Purification, properties, and N-terminal amino acid sequences of five lectins from bark. Plant Physiol. 86: 67–70

    Google Scholar 

  • Ho, S.; Malek-Hedayat, S.; Wang, J. L.; Schindler, M. 1986: Endogenous lectins from cultured soybean cells: isolation of a protein immunologically cross-reactive with seed soybean agglutinin and analysis of its role in binding of Rhizobium japonicum. J. Cell Biol. 103: 1043–1054

    Google Scholar 

  • Horejsí, V.; Haskovec, C.; Kocourek, J. 1978: Studies on lectins XXXVIII. Isolation and characterization of the lectin from black locust bark (Robinia pseudacacia L.). Biochim. Biophys. Acta 532: 98–104

    Google Scholar 

  • Kombrink, E.; Schroder, M.; Hahlbrock, K. 1988: Several “pathogenesis-related” proteins in potato are 1,3-β-glucanases and chitinases. Proc. Nat. Acad. Sci. USA 85: 782–786

    Google Scholar 

  • Kurosaki, F.; Tashiro, N.; Nishi, A. 1988: Role of chitinase and chitin oligosaccharides in lignification response of cultured carrot cells treated with mycelial walls. Plant Cell Physiol. 29: 527–531

    Google Scholar 

  • LeGrand, M.; Kauffmann, S.; Geoffroy, P.; Fritig, B. 1987: Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases. Proc. Nat. Acad. Sci. USA 84: 6750–6754

    Google Scholar 

  • Liener, I. E. 1964: Seed hemagglutinins. Econ. Bot. 18: 27–33

    Google Scholar 

  • 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

    CAS  PubMed  Google Scholar 

  • Mauch, F.; Hadwiger, L. A.; Boller, T. 1988a: Antifungal hydrolases in pea tissue I. Purification and characterization of two chitinases and two β-1,3-glucanases differentially regulated during development and in response to fungal infection. Plant Physiol. 87: 325–333

    Google Scholar 

  • Mauch, F.; Mauch-Mani, B.; Boller, T. 1988b: Antifungal hydrolases in pea tissue II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol. 88: 936–942

    Google Scholar 

  • Mirelman, D.; Galun, E.; Sharon, N.; Lotan, R. 1975: Inhibition of fungal growth by wheat germ agglutinin. Nature 256: 414–416

    Google Scholar 

  • Nasser, W.; de Tapia, M.; Kauffmann, S.; Montasser-Kouhsari, S.; Burkard, G. 1988: Identification and characterization of maize pathogenesis-related proteins. Four maize PR proteins are chitinases. Plant Mol. Biol. 11: 529–538

    Google Scholar 

  • Nsimba-Lubaki, M.; Peumans, W. J. 1986: Seasonal fluctuations of lectins in barks of elderberry (Sambucus nigra) and black locust (Robinia pseudoacacia). Plant Physiol. 80: 747–751

    Google Scholar 

  • Peumans, W. J.; Nsimba-Lubaki, M.; Peeters, B.; Broekaert, W. F. 1985: Isolation and partial characterization of a lectin from ground elder (Aegopodium podagraria) rhizomes. Planta 164: 75–82

    Google Scholar 

  • Putman, L. J.; Laks, P. E.; Pruner, M. S. 1989: Chemical constituents of black locust bark and their biocidal activity. Holzforschung 43: 219–224

    Google Scholar 

  • Quinn, J. M.; Etzler, M. E. 1987: Isolation and characterization of a lectin from the roots of Dolichos biflorus. Arch. Biochem. Biophys. 258: 535–544

    Google Scholar 

  • Schlumbaum, A.; Mauch, F.; Vögeli, U.; Boller, T. 1986: Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365–367

    Google Scholar 

  • Somers, P. J. B.; Yao, R. C.; Doolin, L. E.; McGowan, M. J.; Fukuda, D. S.; Mynderse, J. S. 1987: Method for the detection and quantitation of chitinase inhibitors in fermentation broths; isolation and insect life cycle effect of A82516. J. Antibiotics 40: 1751–1756

    Google Scholar 

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The authors are grateful for support of this project by the Michigan State University/USDA: CSRS Eastern Hardwood Utilization Research Special Grant Program (87-CSRS-2-3056), and to Dr. J. W. Hanover of Michigan State University, Lansing, MI. We also appreciate the technical assistance of Mr. G. Belkola

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Putman, L.J., Pruner, M.S. & Laks, P.E. Properties of protein constituents of black locust bark. Wood Sci.Technol. 25, 1–6 (1991). https://doi.org/10.1007/BF00195551

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