Summary
The seed lectin of the tree legume,Bauhinia purpurea alba, was localized by electron microscopic immunocytochemistry. The pattern of lectin deposition and site of intracellular localization was examined in mid- to late-maturation seeds. The seed tissue was embedded in Lowicryl K4M, the use of which with seed tissues is discussed. Immunocytochemical labeling was accomplished with colloidal gold coupled to a second antibody. The immunocytochemical reaction was specific and sensitive. Protein bodies, Golgi apparatus and Golgi secretion vesicles were densely labeled. Golgi apparatus was oriented such that Golgi secretion vesicles were in close proximity to the protein bodies. The entire Golgi apparatus was labeled with no concentration gradient across the Golgi stack. These observations indicate that the final site of lectin deposition is the protein body, and that the Golgi apparatus plays an essential role in the deposition process.
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Bain, J. M., Mercer, F. V., 1966: Subcellular organization of developing cotyledons ofPisum sativum. Aust. J. biol. Sci.19, 49–67.
Baumgartner, B., Tokuyasu, K. T., Chrispeels, M. J., 1980: Immunocytochemical localization of reserve protein in the endoplasmic reticulum of developing bean (Phaseolus vulgaris) cotyledons. Planta150, 419–425.
Bollini, R., Chrispeels, M. J., 1978: Characterization and subcellular localization of vicilin and phytohemagglutinin, the two major reserve proteins ofPhaseolus vulgaris L. Planta142, 291–298.
— —, 1979: The rough endoplasmic reticulum is the site of reserve protein synthesis in developingPhaseolus vulgaris cotyledons. Planta146, 487–501.
Boulter, D., 1981: Biochemistry of storage protein synthesis and deposition in the developing legume seed. Adv. Bot. Res.9, 1–31.
Carlemalm, E., Garavito, R. M., Villiger, W., 1982: Resin development for electron microscopy and an analysis of embedding at low temperature. J. Microscopy126, 125–143.
Chrispeels, M. J., 1983a: Incorporation of fucose into the carbohydrate moitey of phytohemagglutinin in developingPhaseolus vulgaris cotyledons. Planta157, 57–461.
—, 1983b: The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta158, 140–151.
—,Higgins, T. J. V., 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.
Craig, S., Goodchild, D. J., 1982: Post-embedding immunolabeling. Some effects of tissue preparation on the antigenicity of plant proteins. Eur. J. Cell. Biol.28, 251–256.
— —,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.
—,Millerd, A., 1981: Pea seed storage proteins. Immunocytochemical localization with protein A gold by electron microscopy. Protoplasma105, 333–339.
Dieckert, J. W., Dieckert, M. C., 1976: The chemistry and cell biology of the vacuolar proteins of seeds. J. Food Sci.41, 475–482.
Farquhar, M. F., Palade, G. E., 1981: The Golgi apparatus (complex)-(1954–1981)—from artifact to center stage. J. Cell Biol.91, 77s-103s.
Green, J. R., Northcote, D. H., 1979: Location of fucosyl transferases in the membrane system of maize root cells. J. Cell Sci.40, 235–244.
Harris, N., Boulter, D., 1976: Subcellular organization of developing cotyledons ofPisum sativum. Aust. J. biol. Sci.19, 49–67.
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.
Horisberger, M., Vonlanthen, M., 1980: Ultrastructural localization of soybean agglutinin in thin sections ofGlycine max (soybean) Var.Altona by the gold method. Histochemistry65, 181–186.
Howard, J., Kindinger, J. I., Shannon, K. M., 1979: Conservation of antigenic determinants among different seed lectins. Arch. Biochem. Biophys.192, 457–465.
—,Shannon, L. M., 1977: A rapid quantative and highly specific assay for carbohydrate binding proteins. Anal. Biochem.79, 234–239.
Hurkman, W. J., Beevers, L., 1982: Sequestration of pea reserve protein by rough microsomes. Plant Physiol.69, 1414–1417.
Irimura, T., Osawa, T., 1972: Studies on a hemagglutinin fromBauhiniapurpurea alba seeds. Arch. Biochem. Biophys.151, 475–482.
Manen, J. F., Pusztai, A., 1982: Immunocytochemical localization of lectins in cells ofPhaseolus vulgaris L. seeds. Planta155, 328–334.
Nagahashi, J., Beevers, L., 1978: Subcellular localization of glycosyltransferase involved in glycoprotein biosynthesis in the cotyledons ofPisum sativum L. Plant Physiol.61, 451–459.
Neumann, D., Weber, E., 1978: Formation of protein bodies in the ripening seeds ofVicia faba L. Biochem. Physiol. Pflanzen173, 167–180.
Nieden, V. Z., Neumann, D., Manteuffel, R., Weber, E., 1982: Electron microscopic immunocytochemical localization of storage proteins inVicia faba seeds. Eur. J. Cell Biol.26, 228–233.
Ray, P. M., 1980: Cooperative action of β-glucan synthetase and UDP-xylose xylosyl transferase of Golgi membranes in the synthesis of xyloglucan-like polysaccharide. Biochim. biophys. Acta629, 432–444.
Roth, J., Bendayan, M., Carlemalm, E., Villiger, W., Garavito, M., 1981: Enhancement of structural preservation and immunocytochemical staining in low temperature-embedded pancreatic tissue. J. Histochem. Cytochem.29, 663–671.
Van der Wilden, W., Herman, E. M., Chrispeels, M. J., 1980: Protein bodies of mung bean cotyledons as autophagic organelles. Proc. Natl. Acad. Sci. U.S.A.77, 428–432.
Van Driessche, E., Smets, G., Dejaegere, R., Kanarek, L., 1981: The immunocytochemical localization of lectin in pea seeds (Pisum sativum L.). Planta153, 287–296.
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Herman, E.M., Shannon, L.M. Immunocytochemical evidence for the involvement of golgi apparatus in the deposition of seed lectin ofBauhinia purpurea (Leguminosae) . Protoplasma 121, 163–170 (1984). https://doi.org/10.1007/BF01282309
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DOI: https://doi.org/10.1007/BF01282309