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The immuno-histochemical localization of lectin in pea seeds (Pisum sativum L.)

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Abstract

The lectin from the garden pea (Pisum sativum L.) has been localized at the ultrastructural level by the unlabeled peroxidase-antiperoxidase procedure of L.A. Sternberger et al. (1970, J. Histochem. Cytochem 18, 315–333) in 24 h imbibed seeds. Upon examination by light microscopy and transmission electron microscopy, the lectin was only found in the protein bodies of cotyledons and embryo axis. Cell walls as well as membraneous fractions were completely devoid of lectin. These results are discussed in relation to the possible physiological function of seed lectins.

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Abbreviations

PBS:

phosphate-buffered saline

TBS:

Tris-buffered saline

PAP-complex:

horseradish peroxidase-antihorseradish peroxidase soluble complex

NGS:

normal goat serum

TBS* :

Tris-buffered saline containing 0.5 M NaCl, pH 7.6

References

  • Bain, J.M., Mercer, F.V. (1966) Subcellular organization of the cotyledons in germinating seeds and seedlings of Pisum sativum L. Aust. J. Biol. Sci. 19, 69–84

    Google Scholar 

  • Bhuvaneswari, T.V., Bauer, W.D. (1978) Role of lectins in plantmicroorganism interactions. III. Influence of rhizosphere/rhizoplane culture conditions on the soybean lectin-binding properties of Rhizobia. Plant Physiol. 62, 71–74

    Google Scholar 

  • Bollini, R., Chrispeels, M.J. (1978) Characterization and localization of vicilin and phytohemagglutinin, the two major reserve proteins of Phaseolus vulgaris L. Planta 142, 291–298

    Google Scholar 

  • Bohlool, B.B., Schmidt, E.L. (1974) Lectins: a possible basis for specificity in the Rhizobium-legume root nodule symbiosis. Science 185, 269–271

    Google Scholar 

  • Bong Yul Yoo (1970) Ultrastructural changes in cells of pea embryo radicules during germination. J. Cell Biol. 45, 158–171

    Article  PubMed  Google Scholar 

  • Bowles, D.J., Kauss, H. (1975) Carbohydrate-binding proteins from cellular membranes of plant tissue. Plant Sci. Lett. 4, 411–418

    Article  Google Scholar 

  • Bowles, D.J., Kauss, H. (1976) Characterization, enzymatic and lectin properties of isolated membranes from Phaseolus aureus. Biochim. Biophys. Acta 443, 360–374

    PubMed  Google Scholar 

  • Bowles, D.J., Lis, H., Sharon, N. (1979) Distribution of lectins in membranes of soybean and peanut plants. Planta 145, 193–198

    Google Scholar 

  • Bowles, D.J., Schnarrenberger, C., Kauss, H. (1976) Lectins as membrane components of mitochondria from Ricinus communis. Biochem. J. 160, 375–382

    Google Scholar 

  • Boyd, W.C. (1963) The lectins: their present status. Vox Sang. 8, 1–32

    Google Scholar 

  • Brown, J.C., Hunt, R.C. (1978) Lectins. Int. Rev. Cytol. 52, 277–349

    Google Scholar 

  • Calderon, R.A., Cordoba, F. (1979) Isolation of antibodies specific for the carbohydrate binding site of Concanavalin A. FEBS Lett. 102, 100–102

    Google Scholar 

  • Clarke, A.E., Knox, R.B., Jermyn, M.A. (1975) Localization of lectins in legume cotyledons. J. Cell Sci. 19, 157–167

    Google Scholar 

  • Coulet, M. (1979) Lectines d'hier et d'aujourd'hui. Ann. Immunol. (Paris) 1, 3–16

    Google Scholar 

  • Cuatrecasas, P. (1970) J. Biol. Chem. 245, 3059–3065

    Google Scholar 

  • Dazzo, F.B., Hubbell, D.H. (1975) Concanavalin A: Lack of correlation between binding to Rhizobium and specificity in the Rhizobium-legume symbiosis. Plant Soil 43, 713–717

    Google Scholar 

  • Dazzo, F.B., Yanke, W.E., Brill, W.J. (1978) Trifoliin: A Rhizobium recognition protein from white clover. Biochim. Biophys. Acta 539, 276–286

    Google Scholar 

  • Grube, D. (1980a) Immunoreactivities of Gastrin (G-) cells. I. Dilution-dependent staining of G-cells by antisera and non-immune sera. Histochemistry 65, 223–237

    Google Scholar 

  • Grube, D. (1980b) Immunoreactivities of Gastrin (G-) cells. II. Non-specific binding of immunoglobulins to G-cells by ionic interactions. Histochemistry 66, 149–167

    PubMed  Google Scholar 

  • Hague, D.R. (1975) Studies of storage proteins of higher plants. I. Concanavalin A from three species of the genus Canavalia. Plant Physiol. 55, 636–642

    Google Scholar 

  • Hamblin, J., Kent, S.P. (1973) Possible role of phytohemagglutinin in Phaseolus vulgaris L. Nature New Biol. 245, 28–29

    Google Scholar 

  • Horisberger, M., Vonlanthen, M. (1980) Ultrastructural localization of soybean agglutinin on thin sections of Glycine max (soybean) var. Altona by the gold method. Histochemistry 65, 181–186

    PubMed  Google Scholar 

  • Howard, I.K., Sage, H.J., Horton, C.B. (1972) Studies on the appearance and location of hemagglutinins from a common lentil during the life cycle of the plant. Arch. Biochem. Biophys. 149, 323–326

    Google Scholar 

  • Kauss, H., Glaser, C. (1974) Carbohydrate-binding proteins from plant cell walls and their possible involvement in extension growth. FEBS Lett. 45, 304–307

    Google Scholar 

  • Köhle, H., Kauss, H. (1979) Binding of Ricinus communis agglutinin to the mitochondrial inner membrane as an artifact during preparation. Biochem. J. 184, 721–723

    Google Scholar 

  • Kyne, J.W., Van Der Schaal, A.M., De Vries, G.E. (1980) Pea lectins and the recognition of Rhizobium leguminosarum. Plant Sci. Lett. 18, 65–74

    Article  Google Scholar 

  • Liener, I.E. (1976) Phytochemagglutinins (phytolectins). Annu. Rev. Plant Physiol. 27, 291–319

    Article  Google Scholar 

  • Lis, H., Sharon, N. (1973) The biochemistry of plant lectins (phytohemagglutinins). Annu. Rev. Biochem. 42, 541–574

    Article  PubMed  Google Scholar 

  • Lis, H., Sharon, N. (1977) Lectins, their chemistry and application to immunology. In: The antigens, vol IV, pp. 429–529, Sela, M., ed. Academic Press, New York

    Google Scholar 

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

    Google Scholar 

  • Pueppke, S.G., Bauer, W.G., Keegstra, K., Ferguson, A.L. (1978) Role of lectins in plant-microorganism interactions. II. Distribution of soybean lectin in tissues of Glycine max (L.) Merr. Plant Physiol. 61, 779–784

    Google Scholar 

  • Rougé, M.P., Plantefol, M.L. (1974a) Etude de la phytohémagglutinine des graines de lentille au cours de la germination et des premiers stade du développement de la plante. Evolution dans les cotylédons. C. R. Acad. Sci. Paris, 278D, 449–452

    Google Scholar 

  • Rougé, M.P., Plantefol, M.L. (1974b) Etude de la phytohémagglutinine des graines de lentille au cours de la germination et des premiers stade du développement de la plante. Evolution dans les racines, les tiges et les feuilles. C.R. Acad. Sci. Paris 278D, 3083–3086

    Google Scholar 

  • Rougé, M.P., Plantefol, M.L. (1976) Biosynthèse des hemagglutinines au cours de la maturation des graines de pois. C.R. Acad. Sci. Paris 282D, 621–623

    Google Scholar 

  • Rougé, P., Labroue, L. (1977) Sur le role des phytohémagglutinines dans la fixation spécifique des souches compatibles de Rhizobium leguminosarum sur les pois. C.R. Acad. Sci. Paris 284D, 2423–2426

    Google Scholar 

  • Sharon, N., Lis, H. (1972) Lectins: cell-agglutinating and sugar-specific proteins. Science 177, 949–959

    PubMed  Google Scholar 

  • Sternberger, L.A., Hardy, P.H. Jr., Cuculis, J.J., Meyer, H.G. (1970) The unlabeled antibody enzyme method of immunohistochemistry. J. Histochem. Cytochem. 18, 315–333

    PubMed  Google Scholar 

  • Tully, R.E., Beevers, H. (1976) Protein bodies of castor bean endosperm. Isolation, fractionation and the characterization of protein components. Plant Physiol. 58, 710–716

    Google Scholar 

  • Van Driessche, E., Vandenbranden, S., Kanarék, L. (1978) Improvement of the purification procedure of pea-lectin and considerations on the subunit structure. Arch. Int. Physiol. Biochem. 86, 963–964

    Google Scholar 

  • Wolpert, J.S., Albersheim, P. (1976) Host-symbiont interactions. I. The lectins of legumes interact with the O-antigen-containing lipopolysaccharides of their symbiont Rhizobia. Biochem. Biophys. Res. Comm. 70, 729–737

    PubMed  Google Scholar 

  • Youle, R.J., Huang, A.H.C. (1976) Protein bodies from the endosperm of castor bean. Subfractionation, protein components, lectins, and changes during germination. Plant Physiol. 58, 703–709

    Google Scholar 

  • Yoshida, K. (1978) Novel lectins in the endoplasmatic reticulum of wheat germ and their possible role. Plant Cell Physiol. 19, 1301–1305

    Google Scholar 

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Van Driessche, E., Smets, G., Dejaegere, R. et al. The immuno-histochemical localization of lectin in pea seeds (Pisum sativum L.). Planta 153, 287–296 (1981). https://doi.org/10.1007/BF00384244

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  • DOI: https://doi.org/10.1007/BF00384244

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