Summary
Acid phosphatase localization has been studied, using the lead salt method, in suspension-cultured cells of the wild carrot. Enzyme activity in most of the cells was restricted to the walls and vacuoles. However, in some senescent cells activity was also seen in the nucleus, at one face of the dictyosomes, and in nearby dictyosome-derived vesciles.
The activity in the walls was closely associated with the central portion of the wall which ultimately disintegrates in auxin-containing media. However, the large vesicles which accumulate in this portion of the wall as it breaks down never showed acid phosphatase activity, nor did the multivesicular bodies which appear to transfer vesicular material into the wall space. Although multivesicular bodies in plant cells resemble the multivesicular lysosomes of animal cells, no evidence could be obtained in this study for the presence in such bodies of hydrolytic enzymes.
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References
Balz, H. P.: Intrazelluläre Lokalisation und Funktion von hydrolytischen Enzymen bei Tabak. Planta (Berl.)70, 207–236 (1966).
Berjak, P.: A lysosome-like organelle in the root cap ofZea mays. J. Ultrastruct. Res.23, 233–242 (1968).
Bowes, B. G.: The origin and development of vacuoles inGlechoma hederacea L. Cellule55, 359–364 (1965).
Burstone, M. S.: Enzyme Histochemistry. New York and London: Acad. Press 1962.
Corbett, J. R., andC. A. Price: Intracellular distribution of p-nitrophenyl phosphatase in plants. Plant Physiol.42, 827–830 (1967).
DeJong, D. W., E. F. Jansen, andA. C. Olson: Oxidoreductive and hydroytic enzyme patterns in plant suspension culture cells. Exp. Cell Res.47, 139–156 (1967).
—,A. C. Olson, andE. F. Jansen: Glutaraldehyde activation of nuclear acid phosphatase in cultured plant cells. Science155, 1672–1674 (1966).
Frederick, S. E., E. H. Newcomb, E. L. Vigil, andW. P. Wergin: Fine structural characterization of plant microbodies. Planta (Berl.)81, 229–252 (1968).
Frey-Wyssling, A., E. Grieshaber, andK. Mühlethaler: Origin of spherosomes in plant cells. J. Ultrastruct. Res.8, 506–516 (1963).
Gahan, P. B.: Histochemical evidence for the presence of lysome-like particles in root meristem cells ofVicia faba. J. exp. Bot.16, 350–355 (1965).
—, andA. J. Maple: The behavior of lysosome-like particles during cell differentiation. J. exp. Bot.17, 151–155 (1966).
Gordon, G. B., L. R. Miller, andK. G. Bensch: Studies on the intracellular digestive process in mammalian tissue culture cells. J. Cell Biol.25, 41–55 (1965).
Hall, L. J., andV. S. Butt: Localization and kinetic properties of β-glycerophosphatase in barley roots. J. exp. Bot.19, 276–287 (1968).
Halperin, W., andW. A. Jensen: Ultrastructural changes during growth and embryogenesis in carrot cell cultures. J. Ultrastruct. Res.18, 428–443 (1967).
Holcomb, G. E., A. C. Hildebrandt, andR. F. Evert: Staining and acid phosphatase reactions of spherosomes in plant tissue culture cells. Amer. J. Bot.54, 1204–1209 (1967).
Jensen, T. E., andJ. G. Valdovinos: Fine structure of abcission zones III. Cytoplasmic changes in abscising pedicels of tobacco and tomato flowers. Planta (Berl.)83, 303–313 (1968).
Jensen, W. A.: Composition and ultrastructure of the nucellus in cotton. J. Ultrastruct. Res.13, 112–128 (1965).
Kivilaan, A., T. C. Beaman, andR. S. Bandurski: Enzymatic activities associated with cell wall preparations from corn coleoptiles. Plant Physiol.36, 605–610 (1961).
Lamport, D. T., and D. H. Northcote: The use of tissue cultures for the study of plant cell walls. (Abstr.) Biochem. J.76, 52P (1960).
Lin, M., andE. J. Staba: Peppermint and spearmint tissue cultures I. Callus formation and submerged culture. Lloydia24, 139–145 (1961).
Matile, P.: Aleurone vacuoles as lysosomes. Z. Pflanzenphysiol.58, 365–368 (1968).
—: Lysosomes of root cells in corn seedlings. Planta (Berl.)79, 181–196 (1968).
—, andJ. Spichiger: Lysosomal enzymes in spherosomes (oil droplets) of tobacco endosperm. Z. Pflanzenphysiol.58, 277–280 (1968).
Murashige, T., andF. Skoog: A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plantarum (Cph.)15, 473–497 (1962).
Nougarède, A., J. Guern etC. Grignon: Premières observations sur l'infrastructure des suspensions cellulaires provenant de tissues de cambium d'Acer pseudoplatanus. C. R. Acad. Sci. (Paris)266, 207–210 (1968).
Pease, D. C.: Histological techniques for electron microscopy. New York and London: Acad. Press 1964.
Poux, N.: Localisation de la phosphatase acide dans les cellules meristematiques de Blé (Triticum vulgare). J. Microscopie2, 485–489 (1963).
Robards, A. W.: On the ultrastructure of differentiating secondary xylem in willow. Protoplasm65, 449–464 (1968).
Semadeni, E. G.: Enzymatische Charakterisierung der Lysosomenäquivalente (Sphärosomen) von Maiskeimlingen. Planta (Berl.)72, 91–118 (1967).
Strauss, W.: Lysosomes, phagosomes and related particles. In: Enzyme cytology, p. 239–319 (D. B. Roodyn, ed.). London and New York: Acad. Press 1967.
Sutton-Jones, B., andH. E. Street: Studies on the growth in culture of plant cells III. Changes in fine structure during the growth ofAcer pseudoplatanus cells in suspension culture. J. exp. Bot.19, 114–118 (1968).
Valdovinos, J. G., andT. E. Jensen: Fine structure of abscission zones. II. Cell wall changes in abscising pedicels of tobacco and tomato flowers. Planta (Berl.)83, 295–302 (1968).
Williers, T. A.: Cytolysosomes in long-dormant plant embryo cells. Nature (Lond.)214, 1356–1357 (1967).
Walek-Czernecka, A.: Mise en évidence de la phosphatase acide (monophosphoesterase II) dans les sphérosomes des cellules épidermiques des écailles bulbaire d'Allium cepa. Acta Soc. Bot. Polon.31, 539–543 (1962).
Wardrop, A. B.: Occurrence of structures with lysosome-like function in plant cells. Nature (Lond.)218, 978–980 (1968).
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Halperin, W. Ultrastructural localization of acid phosphatase in cultured cells ofDaucus carota . Planta 88, 91–102 (1969). https://doi.org/10.1007/BF01391115
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DOI: https://doi.org/10.1007/BF01391115