Abstract
The lectin, concanavalin A (Con A), was localized in the cotyledon of developing jack beans (Canavalia ensiformis (L.) DC) by electron-microscope immunocytochemistry. In mature seeds, Con A was present in protein-storage vacuoles (protein bodies) of storage-parenchyma cells. Although protein bodies could be seen in other cell types, only protein bodies in storage-parenchyma cells contained Con A. During seed development, Con A was also localized on the endoplasmic reticulum and Golgi apparatus, presumably en route toward deposition within the protein bodies. The intensity of labeling of the endoplasmic reticulum was much greater during the developmental stage of protein-body filling (66% final seed weight) than in mature seeds.
Similar content being viewed by others
Abbreviations
- Con A:
-
concanavalin A
- ER:
-
endoplasmic reticulum
- IgG:
-
immunoglobulin G
References
Adler, K., Muntz, K. (1983) Origin and development of protein bodies in cotyledons of Vicia faba. Planta 157, 401–410
Bailey, C.J., Cobb, A., Boulter, D. (1970) A cotyledon slice system for the electron autoradiographic study of the synthesis and intracellular transport of seed storage protein of Vicia faba. Planta 95, 103–118
Bain, J.M., Mercer, F.V. (1966) Subcellular organization of developing cotyledons of Pisum sativum. Aust. J. Biol. Sci. 19, 49–67
Barondes, S.H. (1981) Lectins, their multiple endogenous cellular functions. Annu. Rev. Biochem. 50, 207–231
Baumgartner, B., Tokuyasu, K.T., Chrispeels, M.J. (1980) Immunocytochemical localizations of reserve protein in the endoplasmic reticulum of developing bean (Phaseolus vulgaris) cotyledons. Planta 150, 419–425
Beachy, R.N., Thompson, J.R., Madison, J.T. (1978) Isolation of polyribosomes and messenger RNA active in in vitro synthesis of soybean seed proteins. Plant Physiol. 61, 139–144
Bollini, R., Chrispeels, M.J. (1978) Characterization and subcellular localization of vicilin and phytohemagglutinin, the two major reserve proteins of Phaseolus vulgaris L. Planta 142, 291–298
Bollini, R., Chrispeels, M.J. (1979) The rough endoplasmic reticulum is the site of reserve-protein synthesis in developing Phaseolus vulgaris cotyledons. Planta 146, 487–501
Bollini, R., Van der Wilden, W., Chrispeels, M.J. (1982) A precursor of the reserve-protein, Phaseolin, is transiently associated with the endoplasmic reticulum of developing Phaseolus vulgaris cotyledons. Physiol. Plant. 55, 82–92
Briarty, L.G., Coult, D.A., Boulter D. (1973) Protein bodies of developing seeds of Vicia faba. J. Exp. Bot. 20, 289–301
Chrispeels, M.J. (1983) The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta 158, 140–151
Chrispeels, M.J. (1984) Biosynthesis, processing and transport of storage proteins and lectins. Philos. Trans. R. Soc. London Ser. B 304:309–322
Chrispeels, M.J., Bollini, R. (1982) Characteristics of membrane-bound lectin in developing Phaseolus vulgaris cotyledons. Plant Physiol. 70, 1425–1428
Chrispeels, M.J., Higgins, T.J.V., S. Craig, S., Spencer, D. (1982) Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J. Cell Biol. 93, 5–14
Clarke, A.E., Knox, R.B., Jermyn, M.A. (1975) Localization of lectins in legume cotyledons. J. Cell Biol. 19, 157–167
Craig, S., Goodchild, D.J., Hardham, A.R. (1979) Structural aspects of protein accumulation in developing pea cotyledons. I. Qualitative and quantitative changes in parenchyma cell vacuoles. Aust. J. Plant Physiol. 6, 81–98
Cunningham, B.A., Wang, J.L., Waxdal, M.J., Edelman, G.M. (1975) The covalent and three dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3 *. J. Biol. Chem. 250, 1503–1512
Dieckert, J.W., Dieckert, M.C. (1976) The chemistry and cell biology of the vacuolar proteins of seeds. J. Food Sci. 41, 475–482
Harris, N. (1979) Endoplasmic reticulum in developing seeds of Vicia faba. Planta 146, 63–69
Harris, N., Boulter, D. (1976) Protein body formation in cotyledons of developing cowpea (Vigna unguiculata). Ann. Bot. 40, 739–744
Herman, E.M., Shannon, L.M. (1984) The role of the Golgi apparatus in the deposition of the seed lectin of Bauhinia purpurea (Leguminosae). Protoplasma, in press
Higgins, T.J.V., Spencer, D. (1981) Precursor forms of pea vicilin subunits modification by microsomal membranes during cell free translation. Plant Physiol. 65, 205–211
Howard, J., Shannon, L.M. (1977) A rapid quantitative and highly specific assay for carbohydrate binding proteins. Anal. Biochem. 79, 234–239
Howard, J., Kindinger, J.I., Shannon, L.M. (1979) Conservation of antigenic determinants among different seed lectins. Arch. Biochem. Biophys. 192, 457–465
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
Hurkman, W.J., Beevers, L. (1982) Sequestration of pea reserve proteins by rough microsomes. Plant Physiol 69, 1414–1417
Kilpatrick, D.C., Yeoman, M.M., Gould, A.R. (1979) Tissue and subcellular distribution of the lectin from Datura stramonium (Thorn apple). Biochem. J. 184, 215–219
Lis, H., Sharon, N. (1981) Lectins in higher plants. In: The biochemistry of plants, vol. 6, pp. 371–447, Conn, E., Stumpf, P.F., eds. Academic Press, New York London
Manen, J.F., Pusztai, A. (1982) Immunocytochemical localization of lectins in cells of Phaseolus vulgaris L. seeds. Planta 155, 328–334
Mishkind, M., Raikhel, N.V., Palevitz, B.A., Keegstra, K. (1982) Immunocytochemical localization of wheat germ agglutinin in wheat. J. Cell Biol. 92, 753–764
Neumann, D., Weber, E. (1978) Formation of protein bodies in the ripening seeds of Vicia Faba L. Biochem. Physiol. Pflanz. 173, 167–180
Pueppke, S.G., Freidman, H.P., Lee-Chin, S. (1981) Examination of Le and lele genotypes of Glycine max (L.) Merr. for membrane-bound and buffer-soluble soybean lectin. Plant Physiol. 68, 905–909
Spurr, A.R. (1969) A low viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 26, 31–48
Sun, S.M., Buchbinder, B.U., Hall, T.C. (1975) Cell free synthesis of the major storage protein of the bean Phaseolus vulgaris L. Plant Physiol. 56, 780–785
Tully, R.E., Beevers, H. (1976) Protein bodies of castor bean endosperm. Plant Physiol. 58, 710–716
Van Driessche, E., Smets, G., Dejaegcne, R., Kanarsk, L. (1981) The immunohistochemical localization of lectin in pea seeds (Pisum sativum L.). Planta 153, 287–296
Wang, J.L., Cunningham, B.A., Waxdal, M.J., Edelman, G.M. (1975) The covalent and three dimensional structure of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2 *. J. Biol. Chem. 250, 1490–1502
Youle, R.J., Huang, A.H.C. (1976) Protein bodies from the endosperm of castor bean. Plant Physiol. 58, 703–709
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Herman, E.M., Shannon, L.M. Immunocytochemical localization of concanavalin A in developing jack-bean cotyledons. Planta 161, 97–104 (1984). https://doi.org/10.1007/BF00395468
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00395468