Advertisement

The plant proteins and peptides and their localization in cells and tissues

  • E. W. Yemm
Chapter
Part of the Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology book series (532, volume 8)

Abstract

Many of the foundations for the study of the proteins of plant tissues are to be found in the pioneer researches of H. Ritthausen (1862–1912) and of T.B. Osborne (1859–1929). The chief objective of this early work was the separation and purification of proteins from other plant constituents; Osborne (1924) in particular described methods for the preparation of protein from a wide variety of fruits and seeds and put forward a system for the classification of these reserve proteins which is still widely used. The separation of proteins from vegetative plant structures, such as leaves, was systematically investigated by Chibnall and his collaborators. As a result of this work, reviewed by Chibnall (1939), proteins associated with protoplasmic structures of the cytoplasm and chloroplast became accessible for investigation of their physicochemical properties and constituent amino-acids.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literature

  1. Äyräpää, T., and H. Nihlën: Investigation on barley malt amylases and related proteins. Acta chem. scand. (Copenh.) 8, 88–105 (1954).Google Scholar
  2. Bailey, C. H.: The constituents of wheat and wheat products. New York 1944.Google Scholar
  3. Bailey, K.: The denaturation of edestin by acid: T. B. Osborne’s edestan. Biochemic. J. 36, 140–154 (1942).Google Scholar
  4. Bishop, L. R.: The composition and quantitative estimation of barley proteins. J. Inst. Brewing 34, 101 (1928).Google Scholar
  5. Block, R., and D. Bolling: The Amino-acid Composition of Proteins and Foods. 2nd ed. Springfield, Ill.: Charles C. Thomas 1951.Google Scholar
  6. Bonner, J.: Plant Biochemistry. New York: Academic Press Inc. 1950.Google Scholar
  7. Bot, G. M.: The chemical composition of chloroplast granules (grana) in relation to their structure. Chronica Bot. (Waltham, Mass.) 7, 66–67 (1942).Google Scholar
  8. Bricas, E., and Cl. Fromageot: Naturally occuring peptides. Adv. Protein Chem. 8, 1–125 (1953).PubMedCrossRefGoogle Scholar
  9. Brohult, S., and E. Sandegren: Seed Proteins. The Proteins, vol. II, part A, pp. 487–512 (Ed. H. Neurath and K. Bailey). New York: Academic Press Inc. 1954.Google Scholar
  10. Chibnall, A. C.: Protein Metabolism in the Plant. New Haven, Conn.: Yale University Press 1939.Google Scholar
  11. Chibnall, A. C., and S. B. Schryver: Investigation on the nitrogenous metabolism of the higher plants. Part I. The isolation of proteins from leaves. Biochemic. J. 15, 60–75 (1921).Google Scholar
  12. Choh Hag Li: Criteria of the purity of a protein. In Amino-acid and Proteins ed. D. M. Greenberg, p. 487. Springfield, Ill.: C. C. Thomas 1952.Google Scholar
  13. Colowick, S.: Glutathione: proceedings of the symposium held at Ridgefield, Connecticut. New York: Academic Press 1954.Google Scholar
  14. Comar, C. L.: Chloroplast substance of spinach leaves. Bot. Gaz. 104, 122–127 (1942).CrossRefGoogle Scholar
  15. Craig, L. C., J. D. Gregory and G. T. Barry: Studies on polypeptides and amino-acids by countercurrent distribution. Cold Spring Harbour Symp. Quant. Biol. 14, 24–31 (1949).CrossRefGoogle Scholar
  16. Damodaran, M., G. Jaabach and A. C. Chibnall: The isolation of glutamine from an enzymic digest of gliadin. Biochemic. J. 26, 1704–1713 (1932).Google Scholar
  17. Danielsson, C. E.: Seed globulins of the Gramineae and Leguminoseae. (2) Leguminoseae. Biochemic. J. 44, 387 (1949).Google Scholar
  18. An electrophoretic investigation of vicilin and legumin from seeds of peas. Acta chem. scand. (Copenh.) 4, 762–771 (1950).Google Scholar
  19. Danielsson, C. E.: Studies on a proteolytic enzyme from seeds of peas. Acta chem. scand. (Copenh.) 5, 791–804 (1951).CrossRefGoogle Scholar
  20. Investigations on the seed proteins of the Gramineae and Leguminoseae. Sartryck ur Svensk kem. Tidskr. 64, 43–63 (1952).Google Scholar
  21. Dekker, C. A., D. Stone and J. S. Fruton: A peptide from a marine alga. J. of Biol. Chem. 181, 719–729 (1949).Google Scholar
  22. Dowmont, Y. P., and J. S. Fruton: Chromatography of peptides as applied to transamidation reactions. J. of Biol. Chem. 197, 271–283 (1952).Google Scholar
  23. Engel, C., and J. Heins: Distribution of enzymes in resting cereals. II. Distribution of the proteolytic enzymes in wheat, rye and barley. Biochim. et Biophysica Acta 1, 190–196 (1947).CrossRefGoogle Scholar
  24. Folkes, B. F., and E. W. Yemm: The amino-acid content of the proteins of barley grains. Biochemic. J. 62, 4–11 (1956).Google Scholar
  25. Fowden, L.: The composition of the bulk proteins of Chlorella. Biochemic. J. 50, 355–360 (1951).Google Scholar
  26. Fruton, J. S., and S. Simmonds: General Biochemistry. New York: John Wiley & Sons, Inc. 1953.Google Scholar
  27. Gale, E. F.: Assimilation of amino-acids by gram-positive bacteria and some actions of antibiotics thereon. Adv. Protein Chem. 8, 285–391 (1953).PubMedCrossRefGoogle Scholar
  28. Granick, S.: Quantitative isolation of chloroplasts from higher plants. Amer. J. Bot. 25, 558–561 (1938a).CrossRefGoogle Scholar
  29. Chloroplast nitrogen of some higher plants. Amer. J. Bot. 25, 561–567 (1938b).Google Scholar
  30. Gurthrie, J. D.: Isolation of glutathione from potato tubers treated with ethylene chlorohydrin. J. Amer. Chem. Soc. 54, 2566–2567 (1932).CrossRefGoogle Scholar
  31. Haas, P.: On certain peptides occurring in marine algae. Biochemic. J. 46, 503–505 (1950).Google Scholar
  32. Haas, P., and T. G. Hill: Observations on the metabolism of certain seaweeds. Ann. of Bot. 47, 55–67 (1933).Google Scholar
  33. Haas, P., T. G. Hill and B. Russell-Wells: On certain simple peptides occurring in marine algae, Biochemic. J. 32, 2129–2133 (1938).Google Scholar
  34. Hammett, F. S., and S. S. Chapman: A correlation between sulphydryl, mitosis and cell growth in length in roots of Phaseolus vulgaris. Growth 2, 297 (1939).Google Scholar
  35. Hanes, C. S., F. J. R. Hird and F. A. Isherwood: Enzymic transpeptidation reactions involving γ-glutamyl peptides and α-amino-acyl peptides. Biochemic. J. 51, 25–35 (1952).Google Scholar
  36. Harrington, C. R., and T. H. Mead: The synthesis of glutathione. Biochemic. J. 29, 1602–1611 (1935).Google Scholar
  37. Holman, R. T., F. Panzer and B. S. Schweigert: Crystalline lipoxidase. III. Amino-acid composition. Arch. of Biochem. 26, 199–204 (1950).Google Scholar
  38. Hopkins, F. G.: On an autoxidisable constituent of the cell. Biochemic. J. 15, 286–305 (1921).Google Scholar
  39. Hopkins, F. G., and E. J. Morgan: Appearance of glutathione during the early stages of the germination of seeds. Nature (Lond.) 152, 288–290 (1943).CrossRefGoogle Scholar
  40. Irving, G. W., T. D. Fontaine and R. C. Warner: Electrophoretic investigation of peanut protein. I. Peanut meal extract, arachin and conarachin. Arch. of Biochem. 7, 475–489 (1945).Google Scholar
  41. Johns, C. O., and D. B. Jones: The proteins of the peanut, Arachis hypogea, I. The globulins, arachin and conarachin. J. of Biol. Chem. 28, 77–87 (1916).Google Scholar
  42. Johnson, P., F. J. Joubert and E. M. Shooter: Reversible dissociation of arachin. Nature (Lond.) 165, 595 (1950).CrossRefGoogle Scholar
  43. Johnson, P., and W. E. F. Naismith: The physicochemical examination of the conarachin fraction of the groundnut globulins (Arachis hypogaea). Disc. Faraday Soc. 1953, No 13.Google Scholar
  44. Joubert, F. J.: Physicochemical studies of the protein from blue lupin seed (Lupinus angustifolius). Biochim. et Biophysica Acta 16, 370–376 (1954).CrossRefGoogle Scholar
  45. Kendall, E. C., H. L. Mason and B. F. Mc Kenzie: A study of glutathione. III. The structure of glutathione. J. of Biol. Chem. 87, 55–79 (1930a).Google Scholar
  46. A study of glutathione. IV. Determination of the structure of glutathione. J. of Biol. Chem. 88, 409–423 (1930b).Google Scholar
  47. Lawrence, J. M.: Formation of reducing substances in pea seeds. Arch. of Biochem. 27, 1–5 (1950).Google Scholar
  48. Lindan, O., and E. Work: The amino-acid composition of two yeasts used to produce massive dietetic liver necrosis in rats. Biochemic. J. 48, 337–344 (1951).Google Scholar
  49. Lugg, J. H. W.: The representativeness of extracted samples and the efficiency of extraction of protein from fresh leaves of plants; and some partial analyses of the whole proteins of leaves. Biochemic. J. 33, 110–122 (1939).Google Scholar
  50. Plant Proteins. Adv. Protein Chem. 5, 229–304 (1949).Google Scholar
  51. Lugg, J. W. H., and R. A. Weller: Protein in senescent leaves of Trifolium subterraneum: partial amino-acid composition. Biochemic. J. 42, 412–414 (1948).Google Scholar
  52. Lundgren, H. P., and W. H. Ward: Molecular size of proteins. In Amino-acids and Proteins (Ed. D. M. Greenberg). Springfield, Ill.: Charles C. Thomas 1951.Google Scholar
  53. Mazur, A., and H. T. Clarke: The amino-acids of certain marine algae. J. of Biol. Chem. 123, 729–740 (1938).Google Scholar
  54. Chemical components of some autotrophic organisms. J. of Biol. Chem. 143, 39–42 (1942).Google Scholar
  55. Mc Calla, A. G.: Nitrogenous constituents of plants. Annual Rev. Biochem. 18, 615–638 (1949).CrossRefGoogle Scholar
  56. Menke, W.: Untersuchung der einzelnen Zellorgane in Spinatblättern auf Grund präparativ-chemischer Methodik. Z. Bot. 32, 273–295 (1938).Google Scholar
  57. Moore, S., and W. H. Stein: Chromatography of amino-acids on sulfonated polystyrene resins. J. of Biol. Chem. 192, 663–681 (1951).Google Scholar
  58. Moyer, L. S., and M. M. Fishman: The chlorophyll-protein complex. II. Species relationship in certain legumes as shown by electric mobility curves. Bot. Gaz. 104, 449–454 (1942).CrossRefGoogle Scholar
  59. Neish, A. C.: Studies on chloroplasts. I. Separation of chloroplasts, a study of factors affecting their flocculation and the calculation of the chloroplast content of leaf tissue from chemical analysis. Biochemic. J. 33, 293–299 (1939).Google Scholar
  60. Onslow, M. W.: The Principles of Plant Biochemistry. Cambridge: University Press 1931.Google Scholar
  61. Osborne, T. B.: Crystallised vegetable proteids. Amer. Chem. J. 14, 662–689 (1892).Google Scholar
  62. The proteids of barley. J. Amer. Chem. Soc. 17, 539–567 (1895).Google Scholar
  63. The Vegetable Proteins, 2nd. ed. London: Longmans, Green & Co. 1924.Google Scholar
  64. Osborne, T. B., and I. F. Harris: The proteins of the pea (Pisum sativum). J. of Biol. Chem. 3, 213–217 (1907).Google Scholar
  65. Osborne, T. B., and A. J. Wakeman: Proteins of green leaves. I. Spinach leaves. J. of Biol. Chem. 42, 1–26 (1920).Google Scholar
  66. Osborne, T. B., A. J. Wakeman and C. S. Leavenworth: The proteins of the alfalfa plant. J. of Biol. Chem. 49, 63–91 (1921).Google Scholar
  67. Pett, L. B.: Changes in the ascorbic acid and glutathione contents of stored and sprouting potatoes. Biochemic. J. 30, 1228–1232 (1936).Google Scholar
  68. Pirie, N. W.: The criteria of purity used in the study of large molecules of biological origin. Biologic. Rev. 15, 377–404 (1940).CrossRefGoogle Scholar
  69. Quensel, O.: Diss., quoted by Danielsson (1952) (1942).Google Scholar
  70. Rabinowitsch, E. I.: Photosynthesis and Related Processes. New York: Interscience Publication 1945.Google Scholar
  71. Scallet, B. L.: Zein solutions as association-dissociation systems. J. Amer. Chem. Soc. 69, 1602–1608 (1947).CrossRefGoogle Scholar
  72. Schwert, G. W., F. W. Putnam and D. R. Briggs: An electro-phoretic study of gliadin. Arch. of Biochem, 4, 371–387 (1944).Google Scholar
  73. Singer, S. J., L. Eggman, J. M. Campbell and S. G. Wildman: The proteins of green leaves. IV. A high molecular weight protein comprising a large part of the cytoplasmic proteins. J. of Biol. Chem. 197, 233–239 (1952).Google Scholar
  74. Smith, E. L., and R. D. Greene: Further studies on the amino-acid composition of seed globulins. J. of Biol. Chem. 167, 833–842 (1947).Google Scholar
  75. Spragg, S. P.: The metabolism of nitrogen in pea seeds. Ph. D. Thesis, University of Bristol 1955.Google Scholar
  76. Spragg, S. P., and E. W. Yemm: Glutathione and ascorbic acid in the metabolism of germinating peas. Biochemic. J. 58, Proc. Biochem. Soc. XI (1954).Google Scholar
  77. Steward, F. C., and J. F. Thompson: Proteins and protein metabolism in plants. The Proteins, vol. II, part A, pp. 513–594 (Ed. H. Neurath and K. Bailey). New York: Academic Press Inc. 1954.Google Scholar
  78. Sumner, J. B., and F. Somers: Enzymes. New York: Academic Press 1951.Google Scholar
  79. Synge, R. L. M.: Naturally occuring peptides. Quart. Rev. 3, 245 (1949).CrossRefGoogle Scholar
  80. Non-protein nitrogenous constituents of Rye grass: ionophoretic fractionation and isolation of a ‘bound amino-acid’ fraction. Biochemic. J. 49, 642–650 (1951).Google Scholar
  81. Tristram, G. R.: Amino-acid composition of purified proteins. Adv. Protein Chem. 5, 83–153 (1949).CrossRefGoogle Scholar
  82. Vickery, H. B.: The proteins of plants. Physiologic. Rev. 25, 347–376 (1945).Google Scholar
  83. Wildman, S. G., and J. Bonner: The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of spinach cytoplasmic proteins. Arch. of Biochem. 14, 381–413 (1947).Google Scholar
  84. Wildman, S. G., J. M. Campbell and J. Bonner: The proteins of green leaves. II. Purine, Pentose, total phosphorus and acid-labile phosphorus of the cytoplasmic proteins of spinach leaves. Arch. of Biochem. 24, 9–24 (1949).Google Scholar
  85. Wildman, S. G., and A. T. Jagendorf: Leaf proteins. Annual Rev. Plant Physiol. 3, 131–148 (1952).CrossRefGoogle Scholar
  86. Woodward, G. E.: Glyoxalase. HI. Glyoxalase as a reagent for the quantitative micro-estimation of glutathione. J. of Biol. Chem. 109, 1–10 (1935).Google Scholar
  87. Work, T. S.: D- and L-amino-acids in antibiotics. Biochem. Soc. Symposia 1, 61–77 (1948).Google Scholar
  88. Yemm, E. W.: Cellular oxidations and the synthesis of amino-acids and amides in plants. In Recent Developments in Cell Physiology (Ed. J. A. Kitching). London: Butterworth’s Scientific Publications 1954.Google Scholar
  89. Yemm, E. W., and B. F. Folkes: The amino-acids of cytoplasmic and chloroplastic proteins of barley. Biochemic. J. 55, 700–707 (1953).Google Scholar

Copyright information

© Springer-Verlag oHG. Berlin · Göttingen · Heidelberg 1958

Authors and Affiliations

  • E. W. Yemm

There are no affiliations available

Personalised recommendations