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Der Stickstoffumsatz / Nitrogen Metabolism pp 333–342Cite as

Protein symplexes (Conjugated proteins)

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Abstract

Although we know that proteins combine with various non-proteins substances, very little is known about the products formed. Even if a “conjugated protein” can be isolated, we are not always sure whether it is present as such in the living cell or whether it is an artifact produced by the methods of isolation and purification. It is customary to classify conjugated proteins according to the nature of the “prosthetic group”. Accordingly, the following types of conjugated proteins will be discussed in this chapter: (A) glycoproteins, (B) nucleoproteins, (C) lipoproteins, (D) chloroplastin, (E) ironporphyrin complexes (cytochromes, cytochrome oxidase, catalase, peroxidase, leghemoglobin), (F) metal proteins, (G) flavoproteins, and (H) tetrapyrryl-proteins (phycoerythrin, phycocyanin). This classification has merely practical purposes; it must not give the impression that the different classes of “conjugated proteins” are equally well established. Some of the “conjugated proteins” are certainly stoichiometric compounds of a protein with a definite prosthetic group; others seem to be artifacts, the composition of which depends on the isolation procedure. Most of the conjugated proteins were discovered in animal tissues. Until recently, hardly anything was known on protein symplexes occurring in plants. Indeed, only animal products were discussed in the section on conjugated proteins of the „Handbuch der Pflanzenanalyse“ (Bergmann and Zervas 1933).

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Literature

  • Anderson, D. R., J. D. Spikes and R. Lumry: Studies on a reported crystalline chlorophyll-lipoprotein. Biochim. et Biophysica Acta 15, 298 (1954).

    Article  CAS  Google Scholar 

  • Appleby, C. A., and R. K. Morton: Crystalline cytochrome and lactic dehydrogenase of yeast. Nature (Lond.) 173, 749–752 (1954).

    Article  CAS  Google Scholar 

  • Arnon, D. I.: Copper enzymes in isolated chloroplasts. Plant Physiol. 24, 1–15 (1949).

    Article  PubMed  CAS  Google Scholar 

  • Balls, A. K., W. S. Hale and T. H. Harris: A crystalline protein obtained from a lipoprotein of wheat flour. Cereal Chem. 19, 279–287 (1942).

    CAS  Google Scholar 

  • Bergmann, M., u. L. Zervas: Proteins. G. Klein, Handbuch der Pflanzenanalyse, Bd. 4, S. 299–360. 1944.

    Google Scholar 

  • Bertrand, G.: Correlations between the chemical constitution of organic compounds and their oxidiza-bility by laccase. C. r. Acad. Sci. Paris 122, 1132–1134 (1896).

    CAS  Google Scholar 

  • Boeri, E., E. Cutolo, M. Lussati and L. Tosi: Preparation and properties of cytochrome b2 from yeast. Arch. of Biochem. a. Biophysics 56, 487–499 (1955).

    Article  CAS  Google Scholar 

  • Bonner, J., and S. G. Wildman: Enzymic mechanisms in the respiration of spinach leaves. Arch. of Biochem. 10, 497 (1946).

    CAS  Google Scholar 

  • Chargaff, E.: Lipoproteins. Adv. Protein Chem. 1, 1–24 (1946).

    Article  Google Scholar 

  • Recent work on lipoproteins as cellular constituents. Exper. Cell Res., Suppl. 1, 24–31 (1949).

    Google Scholar 

  • The problem of Nucleoproteins. In: Some Conjugated Proteins, pp. 36–42. New Brunswick: Rutgers University Press 1953.

    Google Scholar 

  • Studies on the fractionation and composition of desoxyribonucleic acids. Trans. Faraday Soc. 50, 293–294 (1954).

    Google Scholar 

  • Chargaff, E., and J. N. Davidson: The nucleic acids, chemistry and biology. New York: Academic Press 1955.

    Google Scholar 

  • Chargaff, E.. and E. Vischer: Nucleoproteins, nucleic acids and related substances. Annual Rev. Biochem. 17, 201–226 (1948).

    Article  CAS  Google Scholar 

  • Chiba, Y.: TWO components in crystalline chlorophyll-lipoprotein. Arch. of Biochem. a. Biophysics 54, 83–92 (1955).

    Article  CAS  Google Scholar 

  • Comar, C. L.: Chloroplast substance of spinach leaves. Bot. Gaz. 104, 122 (1942).

    Article  CAS  Google Scholar 

  • Cook, A. H.: Algal pigments and their significance. Biol. Rev. Cambridge Philos. Soc. 20, 115–132 (1945).

    Article  CAS  Google Scholar 

  • Davenport, H. E., and R. Hill: Preparation and some properties of cytochrome f. Proc. Roy. Soc. Lond., Ser. B 139, 327–345 (1952).

    Article  CAS  Google Scholar 

  • Eggman, L., S. J. Singer and S. G. Wildman: The proteins of green leaves. J. of Biol. Chem. 205, 969–983 (1953).

    CAS  Google Scholar 

  • Ellfolk, N., and A. I. Virtanen: The molecular weight of leghemoglobin. Acta chem. scand. (Copenh.) 6, 411–420 (1952).

    Article  CAS  Google Scholar 

  • Elsden, S. R., M. O. Kamen and L. P. Vernon: A new soluble cytochrome. J. Amer. Chem. Soc. 75, 6347–6348 (1953).

    Article  CAS  Google Scholar 

  • Emerson, R., and C. M. Lewis: The photosynthetic efficiency of phycocyanin in Chroococcus and the problem of carotenoid participation in photosynthesis. J. Gen. Physiol. 25, 579–595 (1942).

    Article  PubMed  CAS  Google Scholar 

  • Euler, H. V., L. Heller and K. Högberg: Nucleoproteins from birch pollen. Ark. Kemi (Stockh.) A 26, No 15 (1948).

    Google Scholar 

  • Fishman, M. M., and L. S. Moyer: Electrophoresis of the protein-chlorophyll complex. Science (Lancaster, Pa.) 95, 128–129 (1942).

    CAS  Google Scholar 

  • Galston, A. W., R. K. Bonnichsen and D, I. Arnon: Preparation of highly purified spinach leaf catalase. Acta chem. scand. (Copenh.) 5, 781–790 (1951).

    Article  CAS  Google Scholar 

  • Goddard, D. R.: Cytochrome c and cytochrome oxidase from wheat sperm. Amer. J. Bot. 31, 270–276 (1944).

    Article  CAS  Google Scholar 

  • Gunar, I. I., E. E. Krastina i K. A. Bryushkova: Effect of 2,4-dichloro-phenoxyacetic acid on metabolism in the sunflower. Dokl. Akad. Nauk SSSR. 84, 173–176 (1952).

    PubMed  CAS  Google Scholar 

  • Haas, E., C. Harrer and T. Hogness: Cytochrome reductase. J. of Biol. Chem. 143, 341–349 (1942).

    CAS  Google Scholar 

  • Haglund, H., and A. Tiselius: Zone electrophoresis in a glass powder column. Acta chem. scand. (Copenh.) 4, 957–962 (1950).

    Article  CAS  Google Scholar 

  • Hammarsten, E.: Biological importance of nucleic acid compounds. Biochem. Z. 144, 383–466 (1924).

    CAS  Google Scholar 

  • Haxo, F. T., C. O. O’Heocha and P. Norris: Comparative studies of chromatographically separated phycoerythrins and phycocyanins. Arch. of Biochem. a. Biophysics 54, 162–167 (1955).

    Article  CAS  Google Scholar 

  • Haxo, F. T., and L. R. Blinks: Photosynthetic action spectra of marine algae. J. Gen. Physiol. 33, 389–422 (1950).

    Article  PubMed  CAS  Google Scholar 

  • Hill, R., and K. Bhagvat: Cytochrome oxidase in flowering plants. Nature (Lond.) 143, 726 (1939).

    Article  CAS  Google Scholar 

  • Hill, R., and E. F. Hartree: Hematin compounds in plants. Annual Rev. Plant Physiol. 4, 115 (1953).

    Article  Google Scholar 

  • Holzach, C., and H. Flück: Experiments on the composition and synthesis of the mucins of Tamus communis. Pharmacol. Acta Helvet. 25, 299–336 (1950).

    CAS  Google Scholar 

  • Physicochemical studies concerning the molecular size and form and uniformity of the mucins of Tamus communis. Pharmacol. Acta Helvet. 26, 153–176 (1951).

    Google Scholar 

  • Horowitz, N. H.: The D-aminooxidase of Neurospora. J. of Biol. Chem. 154, 141–149 (1944).

    CAS  Google Scholar 

  • Horvath, A. A.: Proc. of the 6th Pacific Scientific Conf., p. 449, 1939.

    Google Scholar 

  • James, W. O.: Terminal oxidases in the respiration of the embryos and young rats of barley. Proc. Roy. Soc, Lond., Ser. B 141, 289–299 (1953).

    Article  CAS  Google Scholar 

  • Keilin, D.: Cytochrome, a respiratory pigment, common to animals, yeast and higher plants. Proc. Roy. Soc. Lond., Ser. B 98, 312–339 (1925).

    Article  Google Scholar 

  • Keilin, D., and E. F. Hartree: Purification of horse radish peroxidase and comparison of its properties with those of catalase and methemoglobin. Biochemic. J. 49, 88–106 (1951).

    CAS  Google Scholar 

  • Keilin, D., and T. Mann: Properties of laccase from the latex of laquer trees. Nature (Lond.) 145, 304 (1940).

    Article  CAS  Google Scholar 

  • Keilin, D., and J. D. Smith: Hemoglobin and nitrogen fixation in the root nodules of leguminous plants. Nature (Lond.) 159, 692 (1947).

    Article  CAS  Google Scholar 

  • Keilin, D., and Y. L. Wang: Hemoglobin in the root nodules of leguminous plants. Nature (Lond.) 155, 227–229 (1945).

    Article  CAS  Google Scholar 

  • Knaysi, G., R. F. Baker and J. Hillier: A study with the high-voltage electron microscope of the endospore and life cycle of Bacillus mycoides. J. Bacter. 53, 525–537 (1947).

    CAS  Google Scholar 

  • Krasnovskii, A. A., V. B. Evstigneev, G. P. Brin i V. A. Gavrilova: Isolation of phycoerythrin from red algae and its spectral and photochemical properties. Dokl. Akad. Nauk SSSR. 82, 947–950 (1952).

    PubMed  CAS  Google Scholar 

  • Kubo, H.: Hemoprotein from the root nodule of legumes. Acta phytochim. (Tokyo) 11, 195–200 (1937).

    Google Scholar 

  • Kubowitz, F.: The chemical composition of potato oxidase. Biochem. Z. 292, 221–229 (1937).

    CAS  Google Scholar 

  • Kylin, H.: Fysiograf. Sällsk. Lund Förh. 7, 119–123 (1937).

    Google Scholar 

  • Lemberg, R., and J. W. Legge: Hematin compounds and bile pigments. New York: Interscience publishers 1949.

    Google Scholar 

  • Lepeschkin, W. W.: Some aspects of the state of chlorophyll in chloroplasts. Plant Physiol. 24, 175–177 (1949).

    Article  PubMed  CAS  Google Scholar 

  • Little, H. N., and R. H. Burris: Activity of the red pigment from leguminous root nodules. J. Amer. Chem. Soc. 69, 838–841 (1947).

    Article  CAS  Google Scholar 

  • Lockhart, E. E.: Diaphorase. Biochemic. J. 33, 613–617 (1939).

    CAS  Google Scholar 

  • Lubimenko, W. N.: Plastid pigments and their transformation in living plant tissues. Rev. gén. Bot. 40, 23, 88, 146, 226, 303. 372 (1927).

    Google Scholar 

  • Lundegårdh, H.: A new cytochrome in living roots. Nature (Lond.) 173, 939 (1954).

    Article  Google Scholar 

  • Mahler, H. R., and D. E. Green: Metalloflavoproteins and electron transport. Science (Lancaster, Pa.) 120, 7–12 (1954).

    CAS  Google Scholar 

  • Markham, R., and D. J. Smith: Nucleoproteins and viruses. In Neurath-Bailey, Proteins, vol. II, pp. 1–122. 1954.

    Google Scholar 

  • Metzner, H.: Cytochemical investigations on the occurrence of nucleic acids in chloroplasts. Naturwiss. 30, 64–65 (1952).

    Article  Google Scholar 

  • Meyer, K.: Mucoids and glycoproteins. Adv. Protein Chem. 2, 249–275 (1945).

    Article  CAS  Google Scholar 

  • Mucoproteins and mucoids. In: Some Conjugated Proteins, pp. 64–73. New Brunswick: Rutgers University Press 1953.

    Google Scholar 

  • Moriyama, H.: Formation of cell-like mass from lipoproteins of castor beans. Science (Japan) 11, 482–483 (1941).

    CAS  Google Scholar 

  • Nelson, J. M., and C. R. Dawson: Tyrosinase. Adv. Enzymol. 4, 99–152 (1944).

    CAS  Google Scholar 

  • Nicholas, D. J. D., and A. Nason: Molybdenum as constituent of nitrate reductase. J. of Biol. Chem. 207, 353–360 (1954).

    CAS  Google Scholar 

  • Nyman, M. A., and E. Chargaff: On the lipoprotein particles of yeast cells. J. of Biol. Chem. 180, 741–746 (1949).

    CAS  Google Scholar 

  • Okunuki, K.: Acta phytochim. (Tokyo) 11, 249 (1940).

    Google Scholar 

  • Olcott, H. S., and D. K. Mecham: Lipoprotein nature of the glutenin fraction. Cereal Chem. 24, 407–414 (1947).

    CAS  Google Scholar 

  • Packer, L., and W. Vishniac: The specificity of a diphosphopyridine nucleotide-linked hydrogenase. Biochim. et Biophysica Acta 17, 153–154 (1955).

    Article  CAS  Google Scholar 

  • Pirie, N. W.: The isolation from normal tobacco leaves of nucleoproteins with some similarity to plant viruses. Biochemic. J. 47, 614–625 (1950).

    CAS  Google Scholar 

  • Pollister, A. W., and A. E. Mirsky: Nucleoprotamine of trout sperm. J. Gen. Physiol. 30, 101–116 (1946).

    Article  PubMed  CAS  Google Scholar 

  • Powers, W., S. Lewis and C. R. Dawson: Preparation and properties of a highly purified ascorbic acid oxidase. J. Gen. Physiol. 27, 178–180 (1944).

    Google Scholar 

  • Sagastume, C. A., C. Inda and R. Nico: Preparation of lipid-proteins of plant origin. Rec. Fac. Quim., Univ. Nac. La Plate 15, 39–41 (1940).

    CAS  Google Scholar 

  • Scarisbrick, R.: Hematin compounds in plants. Ann. Rep. Chem. Soc. 244, 226–236 (1947).

    Google Scholar 

  • Semenenko, G. L.: Change in the nucleoprotein content of plants in vegetative hybridization. Biokhimya 17, 655–659 (1952).

    CAS  Google Scholar 

  • Sheratt, H. S. A., and W. C. Evans: A crystalline chlorophyll-protein complex from Chlamydomonas. Nature (Lond.) 173, 540 (1954).

    Article  Google Scholar 

  • Smith, E. L.: Action of sodium dodecyl sulfate on the chlorophyll-protein compound of the spinach leaf. J. Gen. Physiol. 24, 583–596 (1941).

    Article  PubMed  CAS  Google Scholar 

  • Stacey, M.: Conjugated proteins. Disc. Faraday Soc. 13, 245–251 (1953).

    Article  Google Scholar 

  • Stern, K. G., G. Goldstein, J. Wagman and J. Schryver: Studies on desoxyribonucleoproteins: isolation and properties of genoprotein T. Federat. Proc. 6, 296 (1947).

    CAS  Google Scholar 

  • Stoll, A.: Chlorophyll. Fortschr. chem. Forsch. 2, 538–608 (1952).

    Article  CAS  Google Scholar 

  • Svedberg, T., and T. Katsurai: The molecular weight of phycocyan and of phycoerythrin from Porphyra tenera and of phycocyan from Aphanizomenon flos aquae. J. Amer. Chem. Soc. 51, 3573 to 3583 (1929).

    Article  CAS  Google Scholar 

  • Takashitma, S.: Chlorophyll-lipoprotein obtained in crystals. Nature (Lond.) 169, 182–183 (1952).

    Article  Google Scholar 

  • Tauber, H.: The interaction of ascorbic acid with enzymes. Erg. Enzymforsch. 7, 301 (1938).

    CAS  Google Scholar 

  • Theorell, H.: Reversible cleavage of a peroxidase. Ark. Kemi (Stockh.) B 14, No 20 (1940).

    Google Scholar 

  • The preparation and some properties of crystalline horseradish peroxidase. Ark. Kemi (Stockh.) A 16, No 2 (1943).

    Google Scholar 

  • Theorell, H., and A. P. Nygaard: The combination of flavin mononucleotide and riboflavin with the protein of the old yellow enzyme. Acta chem. scand. (Copenh.) 8, 1104–1106 (1954).

    Article  Google Scholar 

  • Thomas, J. B., and W. De Rover: On phycocyanin participation in the Hill reaction of the blue-green alga Synechococcus cedrorum. Biochim. et Biophysica Acta 16, 391–395 (1955).

    Article  CAS  Google Scholar 

  • Tonzig, S.: I mucoproteidi e la vita della cellula vegetale. Padua: Libr. Randi 1942.

    Google Scholar 

  • Tueva, O. F., i S. A. Samoilova: Consequences of phosphate and nitrogen starvation in plants. Dokl. Akad. Nauk SSSR. 59, 589–592 (1948).

    CAS  Google Scholar 

  • Vallee, B. L., and F. L. Hoch: Yeast alcohol dehydrogenase, a zinc enzyme. J. Amer. Chem. Soc. 77, 821–822 (1955).

    Article  CAS  Google Scholar 

  • Vernon, L. P.: Cytochrome c content of Rhodospirillum rubrum. Arch. of Biochem. a. Biophysics 43, 492–493 (1953).

    Article  CAS  Google Scholar 

  • Vernon, P. L., and M. D. Kamen: Hematin compounds in photosynthetic bacteria. J. of Biol. Chem. 211, 643, 663 (1954).

    CAS  Google Scholar 

  • Virtanen, A. I., J. Jorma, H. Linkola and A. Linnasalmi: On the relation between nitrogen fixation and leghemoglobin content of leguminous roots. Acta chem. scand. (Copenh.) 1, 90–111 (1947).

    Article  CAS  Google Scholar 

  • Virtanen, A. I., T. Laine and H. Linkola: The green pigments in the root nodules of leguminous plants. Suomen Kemistilehti B 18, 36–38 (1945).

    Google Scholar 

  • Walkin, J. J., and F. A. Schwertz: Chlorophyll monolayers in chloroplasts. J. Gren. Physiol. 37, 111–120 (1953).

    Article  Google Scholar 

  • Warburg, O., u. W. Christian: On a new oxidation enzyme and its absorption spectru. Biochem. Z. 254, 438–458 (1932); 257, 492 (1933); 266, 377 (1933).

    Google Scholar 

  • Westphal, O., O. Lüderitz u. F. Bister: Extraction of bacteria with phenol/ water. Naturforsch. 7b, 148–155 (1952).

    CAS  Google Scholar 

  • Yakushiji, E.: Occurrence of cytochrome in higher plants and algae. Acta phytochim. Tokyo) 8, 325–329 (1935).

    CAS  Google Scholar 

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Authors
  1. Felix Haurowitz
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Editors and Affiliations

  1. University of Wisconsin, 212-A Bacteriology Building, Madison 6, Wisconsin, USA

    Ethel K. Allen (Collaborator in Bacteriology) & O. N. Allen (Professor of Bacteriology) (Collaborator in Bacteriology) &  (Professor of Bacteriology)

  2. Institut für Kulturpflanzenforschung, Deutschen Akademie der Wissenschaften zu Berlin, Gatersleben (Krs. Aschersleben), Deutschland

    Ilse Böttger

  3. Institut für Zellforschung und Genetik, Medizinisches Nobelinstitut, Karolinska Institutet, Stockholm, Schweden

    Torbjörn Caspersson

  4. l’Ecole Nationale de Médecine et de Pharmacie de Rouen, 42, rue Henri Barbusse, Paris V, Frankreich

    Georges Dillemann (Maître de Conférences) (Maître de Conférences)

  5. Staatsinstitut für allgemeine Botanik, Hamburg 36, Jungiusstraße 6, Deutschland

    Horst Engel

  6. Botanisches Institut der Universität, Bonn, Meckenheimer Allee 170, Deutschland

    Hermann Fischer

  7. 37 Wettsteinallee, Basel, Schweiz

    Markus Guggenheim

  8. University College, London, Great Britain

    Paul Haas (Formerly Reader in Plant Biochemistry) (Formerly Reader in Plant Biochemistry)

  9. Department of Chemistry, Indiana University, Bloomington, Indiana, USA

    Felix Haurowitz (Professor of Chemistry) (Professor of Chemistry)

  10. Department of Chemistry, Oregon State College, Corvallis, Oregon, USA

    W. D. Loomis (Assistant Professor) (Assistant Professor)

  11. Staatsinstitut für Allgemeine Botanik, Hamburg 36, Jungiusstraße 6, Deutschland

    Ernst Manshard (Abteilungsvorsteher) (Abteilungsvorsteher)

  12. Plant Physiology Unit, Department of Botany, University of Sydney, N. S. W., Australia

    H. S. McKee (Senior Research Officer) (Senior Research Officer)

  13. Department of Biochemistry, University of Cambridge, Cambridge, Great Britain

    Kenneth McQuellen M. A., Ph. D. (University lecturer in Biochemistry) (University lecturer in Biochemistry)

  14. Staatsinstituts für Allgemeine Botanik und des Botanischen Gartens, Hamburg 36, Jungiusstraße 6, Deutschland

    Walter Mevius (ordentl. Professor der Universität und Direktor) (ordentl. Professor der Universität und Direktor)

  15. Kiel, Gutenbergstraße 76 II, Deutschland

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  16. Halle/Saale, Am Kirchtor 1, Deutschland

    Kurt Mothes

  17. Forschungsabteilung, AB Kabi, Stockholm 30, Schweden

    Niels Nielsen

  18. Department of Botany, University of the Witwatersrand, Johannesburg, South-Africa

    Niilo Rautanen (Lecturer in Biochemistry) (Lecturer in Biochemistry)

  19. Institut für Kulturpflanzenforschung, Gatersleben (Krs. Aschersleben), Deutschland

    Anneliese Romeike

  20. Agrikulturchemischen und Bodenkundlichen Institutes der Universität, Göttingen, Nikolausberger Weg 7, Deutschland

    F. Scheffer (Direktor) (Direktor)

  21. Instituts für Pflanzenernährung und Bodenkunde, Universität Halle, Halle/Saale, Sophienstraße 17, Deutschland

    Karl Schmalfuss (Direktor) (Direktor)

  22. Max-Planck-Institut für Virusforschung, Tübingen, Melanchthonstraße 36, Deutschland

    Gerhard Schramm

  23. Institut für Kulturpflanzenforschung Gatersleben, Deutschen Akademie der Wissenschaften zu Berlin, Gatersleben (Kreis Aschersleben), Deutschland

    Hans-Botho Schröter

  24. Department of Agricultural Botany, School of Agriculture, University of Nottingham, Nottingham, Great Britain

    D. E. G. Sheat

  25. Division of Plant Industry, Commonwealth Scientific and Industrial Research Organisation, Canberra, Australia

    Donald Spencer (Senior Research Officer) (Senior Research Officer)

  26. University College of Swansea, Swansea, Wales, Great Britain

    H. E. Street D. Sc. (London) (Professor of Botany) (Professor of Botany)

  27. Department of Agric. Biochemistry, Biochem-Virus Building, University of California, Berkeley 4, California, USA

    P. K. Stumpf (Professor of Plant Biochemistry) (Professor of Plant Biochemistry)

  28. Instituts für Ernährung Potsdam-Rehbrücke, Deutschen Akademie der Wissenschaften zu Berlin, Potsdam-Rehbrücke, In den Gehren 20, Deutschland

    Kurt Täufel (1. Direktor) (1. Direktor)

  29. King’s College, Newcastle upon Tyne, Great Britain

    Meirion Thomas (Professor of Botany) (Professor of Botany)

  30. Institut für Organische Chemie, Technischen Hochschule, München, Arcisstraße 21, Deutschland

    Ernst Waldschmidt-Leitz

  31. Nuffield Laboratory of Ophthalmology, University of Oxford, Great Britain

    S. G. Waley

  32. Department of Bacteriology, University of Wisconsin, Madison 6, Wisconsin, USA

    P. W. Wilson (Professor of Bacteriology) (Professor of Bacteriology)

  33. Department of Botany, University of Bristol, Bristol 8, Great Britain

    E. W. Yemm

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Haurowitz, F. (1958). Protein symplexes (Conjugated proteins). In: Allen, E.K., et al. Der Stickstoffumsatz / Nitrogen Metabolism. Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology, vol 8. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-94733-9_16

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