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Polyphenol Oxidase

  • Chapter
Genetic Engineering of Plant Secondary Metabolism

Part of the book series: Recent Advances in Phytochemistry ((RAPT,volume 28))

Abstract

Polyphenol oxidases (PPO) catalyze the one- and two- electron oxidation of phenols to quinones at the expense of O2. PPOs are copper metalloproteins catalyzing the o- hydroxylation of a monophenol, followed by its oxidation to the o-diquinone (cresolase activity), or the oxidation of an o-dihydroxyphenol to the o-diquinone (catecholase activity). The quinonoid reaction products formed by PPO are familiar to anyone who has homogenized plant tissues. PPO-generated quinones are highly reactive, electrophilic molecules which covalently modify and crosslink a variety of cellular constituents, including nucleophiles of proteins such as sulfhydryl, amine, amide, indole and imidazole substituents. The formation of quinone adducts (usually brown or black colored) represents the primary detrimental effect of PPO in food processing and postharvest physiology of plant products and is the primary reason for PPO’s importance in food technology.1 Conversely, the potential for quinones to covalently modify and reduce the nutritive value of plant proteins has also generated interest in PPO-based strategies to increase the herbivore resistance of plants.2 Although the function of PPO in plant metabolism is not well understood, the recent cloning of PPO presents opportunities to explore its function in plants as well as to explore the extent, to which its expression can be manipulated. The purpose of this paper is to review current progress toward understanding the structure and function of PPO, and to describe initial results of attempts to modify PPO expression.

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References

  1. MATHEW, A.G., PARPIA, H.A.B. 1971. Food browning as a polyphenol reaction. Adv. Food Res. 19: 75–145.

    Article  CAS  Google Scholar 

  2. DUFFY, S., FELTON, G. 1991. Enzymatic antinutritive defenses of the tomato plant against insects. In: Naturally Occurring Pest Bioregulators, P. Hedin, ed., American Chemical Society, Washington, D.C., pp.166–197.

    Chapter  Google Scholar 

  3. MAYER, A.M., HAREL, E. 1991. Phenoloxidases and their significance in fruit and vegetables. In: Food Enzymology, P.F. Fox, ed., Elsevier, New York, pp. 373–398.

    Google Scholar 

  4. MAYER, A.M., HAREL, E. 1979. Polyphenol oxidases in plants. Phytochemistry 18: 193–215.

    Article  CAS  Google Scholar 

  5. LERCH, K. 1987. Molecular and active site structure of tyrosinase. Life Chem. Rep. 5: 221–234.

    CAS  Google Scholar 

  6. GAYKEMA, W.P.J, HOL, W.G.J., VEREIJKEN, N.M., SOETER,N.M., BAK, H.J., BEINTEMA, J.J. 1984. 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309: 23–29.

    Article  CAS  Google Scholar 

  7. JACKMAN, M.P., HAJNAL, A., LERCH, K. 1991. Albino mutants of Streptomyces glaucescens tyrosinase. Biochem. J. 274:707–713.

    PubMed  CAS  Google Scholar 

  8. HUBER, M., LERCH, K. 1988. Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase. Biochemistry 27: 5610–5615.

    Article  PubMed  CAS  Google Scholar 

  9. LANG, W.H., VAN HOLDE, K.E. 1991. Cloning and sequencing of Octopus dofleini hemocyanin cDNA: derived sequences of functional units Ode and Odf. Proc. Natl. Acad. Sci. USA 88:244–248.

    Article  PubMed  CAS  Google Scholar 

  10. LERCH, K. 1978. Amino acid sequence of tyrosinase from Neurospora crassa. Proc. Natl. Acad. Sci. USA 8:3635–3639.

    Article  Google Scholar 

  11. CARY, J.M., LAX, A.R., FLURKEY, W.H. 1992. Cloning and characterization of cDNA coding for Vicia faba polyphenol oxidase. Plant Mol. Biol. 20: 245–253.

    Article  PubMed  CAS  Google Scholar 

  12. TOLBERT, N.E. 1973. Activation of polyphenol oxidase of chloroplasts. Plant Physiol. 51:234–244.

    Article  PubMed  CAS  Google Scholar 

  13. ROBINSON, S.P., DRY, LB. 1992. Broad bean leaf polyphenol oxidase is a 60-kilodalton protein susceptible to proteolytic cleavage. Plant Physiol. 99: 317–323.

    Article  PubMed  CAS  Google Scholar 

  14. MOORE, B.M., FLURKEY, W.H. 1990. Sodium dodecyl sulfate activation of a plant polyphenoloxidase. J. Biol. Chem. 265:4982–4988.

    PubMed  CAS  Google Scholar 

  15. SANCHEZ-FERRER, A., BRU, R., GARCIA-CARMONA, F. 1989. Novel procedure for extraction of a latent grape polyphenoloxidase using temperature-induced phase separation in Triton X-114. Plant Physiol. 91:1481–1487.

    Article  PubMed  CAS  Google Scholar 

  16. GOLDBECK, J.H., CAMMARATA, K.V. 1981. Spinach thylakoid polyphenol oxidase. Plant Physiol. 67:977–984.

    Article  Google Scholar 

  17. MEYER, H.U., BIEHL, B. 1980. Activities and multiplicity of phenolase from spinach chloroplasts during leaf aging. Phytochemistry 19:2267–2272.

    Article  CAS  Google Scholar 

  18. SWAIN, T., MAPSON, L.W., ROBB, D.A. 1966. Activation of Vicia faba tyrosinase as effected by denaturing agents. Phytochemistry 5:469–482.

    Article  CAS  Google Scholar 

  19. KENTEN, R.H. 1957. Latent phenolase in extracts of broad bean (Vicia faba L.) leaves. 2. Activation by anionic wetting agents. Biochem. J. 86:244–251.

    Google Scholar 

  20. ROBB, D.A., MAPSON, L.W., SWAIN, T. 1964. Activation of the latent tyrosinase of broad bean. Nature 201:503–504.

    Article  CAS  Google Scholar 

  21. SODERHALL, K., CARLBERG, I., ERIKSSON, T. 1985. Isolation and partial purification of prophenoloxidase from Daucus carota L. cell cultures. Plant Physiol. 78:730–733.

    Article  PubMed  CAS  Google Scholar 

  22. SODERHALL, I., BERGENSTRAHLE, A., SODERHALL, K. 1990. Purification and some properties of a Daucus carota lectin which enhances the activation of prophenoloxidase by CaCl2. Plant Physiol. 93:657–661.

    Article  PubMed  CAS  Google Scholar 

  23. FELTON, G., DONATO, K., DEL VECCHIO, R., DUFFEY, S: 1989 Activation of plant foliar oxidases by insect feeding reduces nutritive quality of foliage for noctuid herbivores. J. Chem. Ecol. 15: 2667–2694.

    Article  CAS  Google Scholar 

  24. VAUGHN, K.C., DUKE, S.O. 1984. Function of polyphenol oxidase in higher plants. Physiol. Plant. 60: 106–112.

    Article  CAS  Google Scholar 

  25. HUTCHESON, S.W., BUCHANAN, B.B., MONTALBINI, P. 1980. Polyphenol oxidation by Vicia faba chloroplast membranes. Plant Physiol. 66:1150–1154.

    Article  PubMed  CAS  Google Scholar 

  26. RATHJEN, A.H., ROBINSON, S.P. 1992. Aberrant processing of polyphenol oxidase in variegated grapevine mutant. Plant Physiol. 99: 1619–1625.

    Article  PubMed  CAS  Google Scholar 

  27. FLURKEY, W. 1990. Electrophoretic and molecular weight anomalies associated with broad bean polyphenol oxidase in SDS-PAGE electrophoresis. Phytochemistry 29: 387–391.

    Article  CAS  Google Scholar 

  28. LANKER, T., KING, T., ARNOLD, S., FLURKEY, W. 1987. Active, inactive and in vitro synthesized forms of polyphenoloxidase during leaf development. Physiol. Plant 69: 323–329.

    Article  CAS  Google Scholar 

  29. GANESA, C., FOX, M.T., FLURKEY, W.H. 1992. Microheterogeneity in purified broad bean polyphenol oxidase. Plant Physiol. 98: 472–479.

    Article  PubMed  CAS  Google Scholar 

  30. KOWALSKI, S.P., EANNETTA, N.T., HIRZEL, A.T., STEFFENS, J.C. 1992. Purification and characterization of polyphenol oxidase from glandular trichomes of Solanum berthaultii. Plant Physiol. 100: 677–684.

    Article  PubMed  CAS  Google Scholar 

  31. HAREL, E., MAYER, A.M. 1968. Interconversion of subunits of catechol oxidase from apple chloroplasts. Phytochemistry 7: 199–204.

    Article  CAS  Google Scholar 

  32. HAREL, E., MAYER, A.M., LEHMAN, E. 1973. Multiple forms of Vitis vinifera catechol oxidase. Phytochemistry 12: 2649–2654.

    Article  CAS  Google Scholar 

  33. BOUTHYETTE, P.Y., EANNETTA, N., HANNIGAN, K.J., GREGORY P. 1987. Solanum berthaultii trichomes contain unique polyphenoloxidases and a peroxidase. Phytochemistry 25: 2949–2954.

    Article  Google Scholar 

  34. ROBB, D.A., MAPSON, L.W., SWAIN, T. 1965. On the heterogeneity of the tyrosinase of broad bean (Vicia faba L.). Phytochemistry 4: 731–740.

    Article  CAS  Google Scholar 

  35. FLURKEY,W.H., JEN, J.J. 1980. Purification of peach polyphenol oxidase in the presence of added protease inhibitors. J. Food Biochem. 4:29–41.

    Article  CAS  Google Scholar 

  36. BALASINGHAM, K., FERDINAND, W. 1970. The purification and properties of a ribonucleoenzyme, o-diphenol oxidase from potatoes. Biochem. J. 118: 15–23.

    Google Scholar 

  37. WESCHE-EBELING, P., MONTGOMERY, M.W. 1990. Strawberry polyphenoloxidase: purification and characterization. J. Food Sci. 55: 1315–1319.

    Article  CAS  Google Scholar 

  38. ZAWISTOWSKI, J., BILIADERIS, C.G., MURRAY E.D. 1988. Purification and characterization of Jerusalem artichoke (Helianthus tuberosus L.) polyphenol oxidase. J. Food Biochem. 12: 1–22.

    Article  CAS  Google Scholar 

  39. STELZIG, D.A., AKHTAR, S., RIBEIRO, S. 1972. Catechol oxidase of Red Delicious apple peel. Phytochemistry 11: 535–539.

    Article  CAS  Google Scholar 

  40. MAIONE, T.E., JAGENDORF, A.T. 1984. Partial deglycosylation of chloroplast coupling factor 1 (CF1) prevents the reconstitution of photophosphorylation. Proc. Natl. Acad. Sci. USA 81:3733–3736.

    Article  PubMed  CAS  Google Scholar 

  41. ANGLETON, E.A., FLURKEY, W.H. 1984. Activation and alteration of plant and fungal polyphenoloxidase enzymes in sodium dodecylsulfate electrophoresis. Phytochemistry 23: 2723–2725.

    Article  CAS  Google Scholar 

  42. SEE, Y.P., JACKOWSKI, G. 1989. Estimating molecular weights of polypeptides by SDS gel electrophoresis. In: Protein Structure, A Practical Approach, T.E. Creighton, ed., IRL Press, Oxford, United Kingdom, pp 1–21.

    Google Scholar 

  43. NEWMAN, S.M., EANNETTA, N.T, YU, H., PRINCE, J.P., DE VICENTE, M.C., TANKSLEY, S.D., STEFFENS, J.C. 1993. Organisation of the tomato polyphenol oxidase gene family. Plant Mol. Biol. 21: 1035–1051.

    Article  PubMed  CAS  Google Scholar 

  44. HUNT, M.D., EANNETTA, N.T., YU, H., NEWMAN, S.M., STEFFENS, J.C. 1993. cDNA cloning and expression of potato polyphenol oxidase. Plant Mol. Biol. 21: 59–68.

    Article  PubMed  CAS  Google Scholar 

  45. SHAHAR, T., HENNIG, N., GUTFINGER, T., HAREVEN, D., LIFSCHITZ, E. 1992. The tomato 66.3-kD polyphenoloxidase gene: Molecular identification and developmental expression. Plant Cell 4: 135–147.

    PubMed  CAS  Google Scholar 

  46. YU, H., KOWALSKI, S.P., STEFFENS, J.C. 1992. Comparison of polyphenoloxidase expression in glandular trichomes of Solanum and Lycopersicon. Plant Physiol. 100: 1885–1890.

    Article  PubMed  CAS  Google Scholar 

  47. STEFFENS, J.C., KOWALSKI, S.P., YU, H. 1990. Characterization of glandular trichome and plastid polyphenol oxidases of potato. In: The Molecular and Cellular Biology of the Potato, M. Vayda and W. D. Park, eds., C.A.B. International, Oxon, pp. 103–112.

    Google Scholar 

  48. YU, H. 1992. Cloning, characterization and expression of tomato polyphenol oxidases. Ph. D. thesis. Cornell University, New York, 150 pp.

    Google Scholar 

  49. MAYER, E.M., HAREL, E. 1981. Polyphenol oxidases in fruits-changes during ripening. In: Recent Advances in the Biochemistry of Fruit and Vegetables, J. Friend, M.C. Rhodes, eds., Academic Press, New York, pp 161–180.

    Google Scholar 

  50. LAX, A.R., VAUGHN, K.C. 1991. Co-localization of polyphenol oxidase and photosystem II proteins. Plant Physiol. 96: 26–31.

    Article  PubMed  CAS  Google Scholar 

  51. SHERMAN, T.D., VAUGHN, K.C., DUKE, S.O. 1991. A limited survey of the phylogenetic distribution of polyphenol oxidase. Phytochemistry 30: 2499–2506.

    Article  CAS  Google Scholar 

  52. FLURKEY, W.H. 1986. Polyphenoloxidase in higher plants: immunological detection and analysis of in vitro translation products. Plant Physiol. 81: 614–618.

    Article  PubMed  CAS  Google Scholar 

  53. JEFFERSON, R.A., WILSON, K.J. 1991. The GUS gene fusion system. In: Plant Molecular Biology Manual, S.B. Gelvin, R.A. Schilperoort, and D.P.S. Verma, eds., Kluwer, Boston, pp. B14/1–B14/33.

    Google Scholar 

  54. JEFFERSON, R.A. 1987. Assaying chimeric genes in plants: the GUS gene fusion system. Plant Mol. Biol. Rep. 5: 387–405.

    Article  CAS  Google Scholar 

  55. JEFFERSON, R.A., KAVANAGH, T.A., BEVAN, M.W. 1987. GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker. EMBO J. 6:3901–3908.

    PubMed  CAS  Google Scholar 

  56. FELTON, G.W., WORKMAN, J., DUFFEY, S.S. 1992. Avoidance of antinutritive plant defense: role of midgut pH in Colorado potato beetle. J. Chem. Ecol. 18: 571–583.

    Article  CAS  Google Scholar 

  57. MAYER, A.M. 1987. Polyphenol oxidases in plants - recent progress. Phytochemistry 26: 11–20.

    Article  Google Scholar 

  58. MAYER, A.M. 1964. Factors controlling activity of phenolase in chloroplasts from sugar beet. Israel J. Bot. 13: 74–81.

    Google Scholar 

  59. VAUGHN, K.C., LAX, A.R., DUKE, S.O. 1988. Polyphenol oxidase: The chloroplast oxidase with no established function. Physiol. Plant. 72: 659–665.

    Article  CAS  Google Scholar 

  60. HENRY, E.W., DEPOORE, M.J., O’CONNOR, M.N., DEMORROW, J.M. 1981. Sorbitol-disrupted spinach (Spinacia oleracea L.) chloroplasts: cytochemical localization of polyphenol oxidase in discontinuous sucrose density gradient fractions. J. Submicrosc. Cytol. 13: 365–371.

    CAS  Google Scholar 

  61. LAX, A.R., VAUGHN, K.C., TEMPLETON, G.E. 1984. Nuclear inheritance of polyphenol oxidase in Nicotiana. J. Heredity 75: 285–287.

    CAS  Google Scholar 

  62. KOWALSKI, S.P., BAMBERG, J., TINGEY, W.M., STEFFENS, J.C. 1990. Insect resistance in the wild potato Solanum berthaultiï. inheritance of glandular trichome polyphenol oxidase. J. Heredity 81:475–478.

    CAS  Google Scholar 

  63. FLURKEY, W.H. 1985. In vitro biosynthesis of Vicia faba polyphenol oxidase. Plant Physiol. 79: 564–567.

    Article  PubMed  CAS  Google Scholar 

  64. DE BOER, A.D., WEISBEEK, P.J. 1991. Chloroplast protein topogenesis. Biochim. Biophys. Acta 1071: 221–253.

    Article  Google Scholar 

  65. SAMACH, A., HAREVEN, D., GUTFINGER, T., KEN-DROR, S.,LIFSCHITZ, E. 1991. Biosynthetic threonine deaminase gene of tomato: Isolation, structure and upregulation in floral organs. Proc. Natl. Acad. Sci. USA 88: 2678–2682.

    Article  PubMed  CAS  Google Scholar 

  66. HALPIN, C., MUSGROVE, J.E., LORD, J.M., ROBINSON, C. 1989.Import and processing of proteins by castor bean leucoplasts. FEBS Letters 258: 32–34.

    Article  CAS  Google Scholar 

  67. STEELE, J. A., UCHYTIL, T.F., DURBIN, R.D., BHATNAGAR, P.,RICH, D.H. 1976. Chloroplast coupling factor 1: A species-specific receptor for tentoxin. Proc. Natl. Acad. Sci. USA 73: 2245–2248.

    Article  PubMed  CAS  Google Scholar 

  68. VAUGHN, K.C., DUKE, S.O. 1981. Tentoxin-induced loss of plastidic polyphenol oxidase. Physiol. Plant. 53: 421–428.

    Article  CAS  Google Scholar 

  69. VAUGHN, K.C., DUKE, S.O. 1984. Tentoxin stops the processing of polyphenol oxidase into an active protein. Physiol. Plant. 60: 257–261.

    Article  CAS  Google Scholar 

  70. KUBOWITZ, F. 1938. Spaltung und Resynthese der Polyphenoloxidase an des Haemocyanins. Biochem. Z. 299: 299–232.

    Google Scholar 

  71. HIBINO, T., DE BOER, A.D., WEISBEEK, P.J., TAKABE, T. 1991.Reconstitution of mature plastocyanin from precursor apo-plastocyanin expressed in Escherichia coli. Biochim. Biophys. Acta 1058: 107–112.

    Article  PubMed  CAS  Google Scholar 

  72. MERCHANT, M., BOGORAD, L. 1986. Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardii. Mol. Cell Biol. 6:462–469.

    PubMed  CAS  Google Scholar 

  73. TINGEY, W.M. 1991. Potato glandular trichomes. In: Naturally Occurring Pest Bioregulators, P.A. Hedin, ed., American Chemical Society, Washington, D.C., pp. 126–135.

    Chapter  Google Scholar 

  74. DUFFEY, S.S. 1986. Plant glandular trichomes: their partial role in defense against insects. In: The Plant Surface and Insects, B. E. Juniper and T. R. E. Southwood, eds., Blackwell, Oxford, pp. 157–178.

    Google Scholar 

  75. RYAN, J.D., GREGORY, P., TINGEY, W.M. 1983. Glandular trichomes: enzymatic browning assays for improved selection of resistance to the green peach aphid. Am. Potato J. 60: 861–868.

    Article  Google Scholar 

  76. RYAN, J.D., GREGORY, P., TINGEY, W.M. 1982. Phenolic oxidase activities in glandular trichomes of Solanum berthaultii. Phytochemistry 21: 1885–1887.

    Article  CAS  Google Scholar 

  77. GREGORY, P., TINGEY, W.M., AVE, D.A., BOUTHYETTE, P.Y.1986. Potato glandular trichomes: A physiochemical defense mechanism against insects. In: Natural Resistance of Plants to Pests. Roles of Allelochemicals, M. B. Green and P. A. Hedin, eds., American Chemical Society, Washington, D.C., pp. 160–167.

    Chapter  Google Scholar 

  78. GIBSON, R.W., TURNER, R.H., 1977. Insect-trapping glandular hairs on potato plants. Proc. Natl. Acad. Sci. USA 23: 272–277.

    Google Scholar 

  79. KOWALSKI, S.P., PLAISTED, R.L., STEFFENS, J.C. 1993.Immunodetection of polyphenol oxidase in glandular trichomes of Solanum berthaultii, S. tuberosum and their hybrids. Am. Potato J. 70: 185–199.

    Article  CAS  Google Scholar 

  80. KOWALSKI, S.P. 1989. Insect resistance in potato: purification and characterization of a polyphenol oxidase from type A glandular trichomes of Solanum berthaultii Hawkes. Ph.D. thesis. Cornell University. 156 pp.

    Google Scholar 

  81. PLAISTED, R.L., TINGEY, W.M., STEFFENS, J.C. 1992. The germplasm release of NYL 235-4, a clone with resistance to the Colorado potato beetle. Am. Potato J. 69: 843–846.

    Article  Google Scholar 

  82. NEAL, J.J., STEFFENS, J. C., TINGEY, W.M. 1989. Glandular trichomes of Solanum berthaultii and resistance to the Colorado potato beetle. Entomol. exp. appl. 59: 133–140.

    Article  Google Scholar 

  83. DIMOCK, M.B., TINGEY, W.M. 1988. Host acceptance behavior of Colorado potato beetle larvae influenced by potato glandular trichomes. Physiol. Entomol. 13: 399–406.

    Article  Google Scholar 

  84. BRODERICK, B., STRONG, D. 1987. Amino acid nutrition of herbivorous insects and stress to host plants. In: Insect Outbreaks, P. Barbosa and J.C. Schultz, eds, Academic press, N.Y., pp. 347–365.

    Google Scholar 

  85. WALDBAUER, G.P. 1968. The consumption and utilization of food by insects. Adv. Insect Physiol. 5: 229–288.

    Article  Google Scholar 

  86. WOLFSON, J.L., MURDOCK, L.L. 1987. Suppression of larval Colorado potato beetle growth and development by digestive proteinase inhibitors. Entomol. Exp. Appl. 44: 235–240.

    Article  CAS  Google Scholar 

  87. CANNON, M., PLATZ, J., O’LEARY, M., SOOKDEO, C., CANNON, F. 1990. Organ-specific modulation of gene expression in transgenic plants using antisense RNA. Plant Mol. Biol. 15: 39–47.

    Article  PubMed  CAS  Google Scholar 

  88. VAN DER KROL, A.R., MUR, L.A., DE LANGE, P., MOL, J.N.M.,STUITJE, A.R. 1990. Inhibition of flower pigmentation by antisense CHS genes: promoter and minimal sequence requirements for the antisense effect. Plant Mol. Biol. 14: 457–466.

    Article  PubMed  Google Scholar 

  89. SANDLER, S.J., STAYTON, M., TOWNSEND, J.A., RALSTON,M.C., BEDBROOK, J.R., DUNSMUIR, P. 1988. Inhibition of gene expression in transformed plants by antisense RNA. Plant Mol. Biol. 11: 301–310.

    Article  CAS  Google Scholar 

  90. HOOKER, W.J. 1987. Tuber diseases. In: Potato Processing, W.F.Talburt and O. Smith, eds., Van Nostrand Reinhold Company, N.Y., pp 149–181.

    Google Scholar 

  91. RICH, A.E. 1983. Potato diseases, Academic Press, N.Y., 238 pp.

    Google Scholar 

  92. STARK, J.C., CORSINI, D.L., HURLEY, P.J., DWELLE, R.B. 1985.Biochemical characteristics of potato clones differing in blackspot susceptibility. Am. Potato J. 62:657–666.

    Article  CAS  Google Scholar 

  93. MAPSON, L.W., SWAIN, T., TOMALIN, A.W. 1963. Influence of variety, cultural conditions and temperature of storage on enzymic browning of potato tubers. J. Sci. Fd Agric. 14:673–684.

    Article  CAS  Google Scholar 

  94. MATHEIS, G. 1987. Polyphenol oxidase and enzymatic browning of potatoes (Solanum tuberosum). II. Enzymatic browning and potato constituents. Chem. Mikrobiol. Technol. Lebensm. 11: 33–41.

    CAS  Google Scholar 

  95. KUNKEL, R., GARDNER, W.H. 1965. Potato tuber hydration and its effect on blackspot of Russet Burbank potatoes in the Columbia River Basin. Am. Potato J. 42:109–124.

    Article  CAS  Google Scholar 

  96. REEVE, R.M. 1968. Preliminary histological observation on internal blackspot in potatoes. Am. Pot. J. 45: 157–167.

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Plant Breeding and Biometry, Cornell University, 252 Emerson Hall, Ithaca, NY, 14853-1901, USA

    John C. Steffens & Michelle D. Hunt

  2. Institute of Life Sciences, Department of Botany, The Hebrew University of Jerusalem, Jerusalem, Israel, 91904

    Eitan Harel

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  1. John C. Steffens
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Editors and Affiliations

  1. University of British Columbia, Vancouver, British Columbia, Canada

    Brian E. Ellis

  2. Applied Biosystems, Foster City, California, USA

    Gary W. Kuroki

  3. Reed College, Portland, Oregon, USA

    Helen A. Stafford

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J.C.S. dedicates this chapter to the memory of Frederick Steffens

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Steffens, J.C., Harel, E., Hunt, M.D. (1994). Polyphenol Oxidase. In: Ellis, B.E., Kuroki, G.W., Stafford, H.A. (eds) Genetic Engineering of Plant Secondary Metabolism. Recent Advances in Phytochemistry, vol 28. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2544-8_11

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