Summary
Some photosynthetic and biochemical properties of the chlorophyl containing layers of the pericarp of developing barley have been investigated. The tissue changes from pale green to bright green early in development, chlorophyll disappearing only at the later stages of maturity. It contains chloroplasts and probably amyloplasts and starch bearing chloroplasts. It is capable of high rates of light dependent oxygen evolution. It has been shown that the enzyme phosphoenol pyruvate carboxylase (EC 4.1.1.31) is present in the pericarp and is 100 times as active in carbon dioxide fixation as ribulose diphosphate carboxylase (EC 4.1.1.39). Other enzymes present in the pericarp are phosphoenol pyruvate synthetase, pyrophosphatase (EC 3.6.1.1), malate NAD and NADP dehydrogenases (EC 1.1.1.37), malic enzyme (EC 1.1.1.40), and fructose 1,6 diphosphatase (EC 3.1.3.11).
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Abbreviations
- RDP:
-
Ribulose 1,5-diphosphate
- PEP:
-
phosphoenol pyruvate
References
Allen, R. J. L.: The estimation of phosphorus. Biochem. J. 34, 858–865 (1940)
Archbold, H. K.: Physiological studies in plant nutrition. XIII. Experiments with barley on defoliation and shading of the ear in relation to sugar metabolism. Ann. Bot., NS. 6, 487–531 (1942)
Arnon, D. I.: Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris. Plant Physiol 24, 1–15 (1949)
Baldry, C. W., Bucke, C., Coombs, J., Gross, D.: Phenols, phenol oxidase and photosynthetic activity of chloroplasts isolated from sugar cane and spinach. Planta (Berl) 94, 107–123 (1970)
Banks, W, Evers, A. D., Muir, D. D.: The location of alpha-amylase in developing cereal grains. Chem. and Ind. No 14, 573–574 (1972)
Baxter, E. D., Duffus, C. M.: Enzymes of carbohydrate metabolism in developing Hordeum distichum grain. Phytochemistry 12, 1923–1928 (1973)
Bergal, P., Clemencet, M.: The botany of the barley plant. In: Barley and malt, p. 1–23 (A. H. Cook, ed.). New York: Academic Press 1962
Buttrose, M. S., May, L. H.: Physiology of cereal grain 1. The source of carbon for the developing barley kernel. Aust. J. biol. Sci. 12, 40–52 (1959)
Calvin, M., Pon, N. G.: Carboxylations and decarboxylations. J. cell. comp. Physiol. 54, Suppl. 1, 51–74 (1959)
Carr, D. J., Wardlaw, I. F.: The supply of photosynthetic assimilates to the grain from the flag leaf and ear of wheat. Aust. J. biol. Sci. 18, 711–719 (1965)
Cockburn, W. C., Baldry, C. W., Walker, D. A.: Some effects of inorganic phosphate on O2 evolution by isolated chloroplasts. Biochim. biophys. Acta (Amst.) 143, 614–624 (1967)
Cooper, R. A., Kornberg, H. L.: Net formation of phosphoenol pyruvate from pyruvate by Escherichia coli. Biochim. biophys. Acta (Amst.) 104, 618–620 (1965)
Duffus, C. M.: Alpha-amylase in the developing barley grain and its dependence on gibberellic acid. Phytochemistry 8, 1205–1209 (1969)
Duffus, C., Rosie, R.: Starch hydrolysing enzymes in the developing barley grain. Planta (Berl.) 109, 153–160 (1973)
Evans, L. T., Rawson, H. M.: Photosynthesis and respiration by the flag leaf and components of the ear during grain development in wheat. Aust. J. biol. Sci. 23, 245–254 (1970)
Frey-Wyssling, A., Buttrose, M. A.: Photosynthesis in the ear of barley. Nature (Lond.) 184, 2031–2032 (1959)
Hatch, M. D., Slack, C. R.: A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role in the C4 dicarboxylic acid pathway of photosynthesis. Biochem. J. 106, 141–146 (1968)
Heppel, L. A.: Inorganic pyrophosphatase from yeast. In: Methods in enzymology, II, p. 570–576 (S P. Colowick, N. O. Kaplan, eds.). New York: Academic Press 1955
Mehler, A. H., Kornberg, A., Grisolia, S., Ochoa, S.: The enzymatic mechanism of oxidation reductions between malate or isocitrate and pyruvate. J. biol. Chem. 174, 961–977 (1948)
Merritt, N. R., Walker, J. T.: Development of starch and other components in normal and high amylose barleys. J. Inst. Brewing 75, 156–164 (1969)
Ochoa, S., Mehler, A. H., Kornberg, A.: Biosynthesis of dicarboxylic acids by carbon dioxide fixation. 1. Isolation and properties of an enzyme from pigeon liver catalysing the reversible decarboxylation of malic acid. J. biol. Chem. 174, 979–1000 (1948)
Racker, E., Schroeder, E. A. R.: The reductive pentose phosphate cycle. II. Specific C-1 phosphatases for fructose, 1,6-diphosphate and sedoheptulose 1,7-diphosphate. Arch. Biochem. Biophys. 74, 326–344 (1958)
Slack, C. R., Hatch, M. D.: Comparative studies on the activity of carboxylases and other enzymes in relation to the new pathway of photosynthetic carbon dioxide fixation in tropical grasses. Biochem. J. 103, 660–665 (1967)
Tolbert, N. E.: Activation of polyphenol oxidase of chloroplasts. Plant Physiol. 51, 234–244 (1973)
Trebst, A.: Measurement of Hill reactions and photoreduction. In: Methods in enzymology, XXIV, p. 146–165 (S. P. Colowick, N. O. Kaplan, eds.) New York: Academic Press 1972
Walker, D. A., Baldry, C. W., Cockburn, W.: Photosynthesis by isolated chloroplasts, simultaneous measurement of carbon assimilation and oxygen evolution. Plant Physiol. 43, 1419–1422 (1968)
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Duffus, C.M., Rosie, R. Some enzyme activities associated with the chlorophyll containing layers of the immature barley pericarp. Planta 114, 219–226 (1973). https://doi.org/10.1007/BF00389037
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DOI: https://doi.org/10.1007/BF00389037