Advertisement

Toxic Extracellular Enzymes

  • H. M. Kalisz
  • M. E. Kalisz
Part of the Modern Methods of Plant Analysis book series (MOLMETHPLANT, volume 13)

Abstract

This Chapter describes the methods used for the assay, identification and determination of “toxic” action of extracellular enzymes of microbial (mainly fungal) and higher plant origin involved in plant pathogenesis. Methods used for the general characterization of an enzyme, such as its catalytic properties, molecular weight, amino acid composition, protein sequence analysis, have been omitted. A detailed account of the theoretical and practical aspects of enzyme characterization may be found in most biochemical textbooks (e.g., Segel 1975; Cornish-Bowden 1979; Page 1984; Darbre 1986; Franks 1988).

Keywords

Chitinase Activity Veratryl Alcohol Glucanase Activity Pectate Lyase Fusarium Solani 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Abu-Goukh AA, Greve LC, Labavitch JM (1983) Purification and partial characterisation of “Bartlett” pear fruit polygalacturonase inhibitors. Physiol Plant Pathol 23: 111–122Google Scholar
  2. Akazawa T, Hara-Nishimura I (1985) Topographic aspects of biosynthesis, extracellular secretion and intracellular storage of proteins in plant cells. Annu Rev Plant Physiol 36: 441–472Google Scholar
  3. Albertsson PA (1986) Partition of cell particles and macromolecules, 3rd edn. J Wiley and Sons, New YorkGoogle Scholar
  4. Andrews AT (1986) Electrophoresis — theory, techniques, and biochemical and clinical applications. Clarendon, OxfordGoogle Scholar
  5. Andro T, Chambost J-P, Kotoujansky A, Cattaneo J, Bertheau Y, Barras F, Van Gijsegem F, Coleno A (1984) Mutants of Erwinia chrysanthemi defective in secretion of pectinase and cellulase. J Bacteriol 160: 1199–1203PubMedGoogle Scholar
  6. Bailey JA, Mansfield JW (eds) (1982) Phytoalexins. J Wiley and Sons, New YorkGoogle Scholar
  7. Beisiegel U (1986) Protein blotting. Electrophoresis 7: 1–18Google Scholar
  8. Bell AA (1981) Biochemical mechanisms of disease resistance. Annu Rev Plant Physiol 32: 21–81Google Scholar
  9. Benhamou N, Grenier J, Asselin A, Legrand M (1989) Immunogold localization of ß-1,3-glucanases in two plants infected by vascular wilt fungi. Plant Cell 1: 1209–1221PubMedGoogle Scholar
  10. Benhamou N, Joosten MHAJ, De Wit PJGM (1990) Subcellular localization of chitinase and of its potential substrate in tomato root tissues infected by Fusarium oxysporum f. sp. radicis-lycopersici. Plant Physiol 92: 1108–1120PubMedGoogle Scholar
  11. Biely P, Markovic O, Mislovicovd D (1985) Sensitive detection of endo-1,4–13-glucanases and endo-1,4–13-xylanases in gels. Anal Biochem 144: 147–151PubMedGoogle Scholar
  12. Boller T (1986) Role of proteolytic enzymes in interactions of plants with other organisms. In: Dalling M (ed) Plant proteolytic enzymes. CRC Press, Boca Raton, FloridaGoogle Scholar
  13. Boller T (1987) Hydrolytic enzymes in plant disease resistance. In: Kosuge T, Nester EW (eds) Plant-microbe interactions, molecular and genetic perspectives, vol 2. Macmillan, New York, pp 385–414Google Scholar
  14. Boller T, Mauch F (1988) Colorimetric assay for chitinase. Methods Enzymol 161: 430–435Google Scholar
  15. Boller T, Métraux JP (1988) Extracellular localization of chitinase in cucumber. Physiol Mol Plant Pathol 33: 11–16Google Scholar
  16. Boller T, Gehri A, Mauch F, Vögeli U (1983) Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157: 22–31Google Scholar
  17. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254PubMedGoogle Scholar
  18. Broekaert WF, Van Parijs J, Allen AK, Peumans WJ (1988) Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol Mol Plant Pathol 33: 319–331Google Scholar
  19. Broekaert WF, Van Parijs J, Leyns F, Joos H, Peumans WJ (1989) A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science 245: 1100–1102PubMedGoogle Scholar
  20. Brown RE, Jarvis KL, Hyland KJ (1989) Protein measurement using bicinchoninic acid: elimination of interfering substances. Anal Biochem 180: 136–139PubMedGoogle Scholar
  21. Burnette WN (1981) “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate — polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodicated protein A. Anal Biochem 112:195–203Google Scholar
  22. Cabib E (1988) Assay for chitinase using tritiated chitin. Methods Enzymol 161: 424–426Google Scholar
  23. Canevascini G, Gattlen C (1981) A comparative investigation of various cellulase assay procedures. Biotechnol Bioeng 23: 1573–1590Google Scholar
  24. Chatterjee AK, Starr MP (1977) Donor strains of the soft-rot bacterium Erwinia chrysanthemi and conjugational transfer of the pectolytic capacity. J Bacteriol 132: 862–862PubMedGoogle Scholar
  25. Chavira R, Burnett TJ, Hageman JH (1984) Assaying proteinases with Azocoll. Anal Biochem 136: 446–450PubMedGoogle Scholar
  26. Clancy FG, Coffey D (1977) Acid phosphatase and protease release by the insectivorous plant Drosera rotundifolia. Can J Bot 55: 480–488Google Scholar
  27. Collmer A (1987) Pectic enzymes and bacterial invasion of plants. In: Kosuge T, Nester EW (eds) Plant-microbe interactions, molecular and genetic perspectives, vol 2. Macmillan, New York, pp 253–284Google Scholar
  28. Collmer A, Keen NT (1986) The role of pectic enzymes in plant pathogenesis. Annu Rev Phytopathol 24: 383–409Google Scholar
  29. Collmer A, Schoedel C, Roeder DL, Ried JL, Rissler JF (1985) Molecular cloning in Escherichia colt of Erwinia chrysanthemi genes encoding multiple forms of pectate lyase. J Bacteriol 161: 913–920PubMedGoogle Scholar
  30. Collmer A, Ried JL, Mount MS (1988) Assay methods for pectic enzymes. Methods Enzymol 161: 329–335Google Scholar
  31. Cornish-Bowden A (1979) Fundamentals of enzyme kinetics. Butterworths, LondonGoogle Scholar
  32. Coté F, Letarte J, Grenier J, Trudel J, Asselin A (1989) Detection of 13–1,3-glucanase activity after native polyacrylamide gel electrophoresis: application to tobacco pathogenesis-related proteins. Electrophoresis 10: 527–529PubMedGoogle Scholar
  33. Coughlan MP (1988) Staining techniques for the detection of the individual components of cellulolytic enzyme systems. Methods Enzymol 160: 135–144Google Scholar
  34. Cutting JA (1984) Gel protein stains: phosphoproteins. Methods Enzymol 104: 451455Google Scholar
  35. Darbre A (ed) (1986) Practical protein chemistry — a handbook. Wiley and Sons, New YorkGoogle Scholar
  36. Darvill AG, Albersheim P (1984) Phytoalexins and their elicitors — a defence against microbial infection in plants. Annu Rev Plant Physiol 35: 243–275Google Scholar
  37. Dean RA, Timberlake WE (1989) Regulation of the Aspergillus nidulans pectate lyase gene (pe1A). Plant Cell 1: 275–284PubMedGoogle Scholar
  38. Dey PM, Campillo ED (1984) Biochemistry of the multiple forms of glycosidases in plants. Adv Enzymol Relat Areas Mol Biol 56: 141–249PubMedGoogle Scholar
  39. Dickman MB, Patil SS, Kolattukudy PE (1982) Purification and characterization of an extracellular cutinolytic enzyme from Colletotrichum gloeosporioides on Carica papaya. Physiol Plant Pathol 29: 333–347Google Scholar
  40. Dickman MB, Podila GK, Kolattukudy PE (1989) Insertion of cutinase gene into a wound pathogen enables it to infect intact host. Nature 342: 446–448Google Scholar
  41. Doerner KC, White BA (1990) Detection of glycoproteins separated by nondenaturing polyacrylamide gel electrophoresis using the periodic acid-Schiff stain. Anal Biochem 187: 147–150PubMedGoogle Scholar
  42. Dunn MJ (ed) (1986) Gel electrophoresis of proteins. Wright, BristolGoogle Scholar
  43. Edreva AM, Georgieva ID (1980) Biochemical and histochemical investigations of a-and (3-glucosidase activity in an infectious disease, a physiological disorder and in senescence of tobacco leaves. Physiol Plant Pathol 17: 237–243Google Scholar
  44. Eriksson K-E, Blanchette RA, Ander P (1990) Microbial and enzymatic degradation of wood and wood components. Springer, Berlin Heidelberg New YorkGoogle Scholar
  45. Eriksson S, Bhikhabhai R, Hammar L (1989) Analysis of glycoproteins — lectin binding of HIV glycoproteins. PhastSystem Application File No. 301, Pharmacia LKB Biotechnology, Uppsala, SwedenGoogle Scholar
  46. Etzler ME (1985) Plant lectins: molecular and biological aspects. Annu Rev Plant Physiol 36: 209–234Google Scholar
  47. Evans CH, Ridella JD (1984) An evaluation of fluorometric proteinase assays which employ fluorescamine. Anal Biochem 142: 411–420PubMedGoogle Scholar
  48. Flurkey WH, Kolattukudy PE (1981) In vitro translation of cutinase in mRNA: evidence for a precursor form of an extracellular fungal enzyme. Arch Biochem Biophys 212: 154–161PubMedGoogle Scholar
  49. Franks F (ed) (1988) Characterisation of proteins. Human Press, Clifton, New JerseyGoogle Scholar
  50. Friedenauer S, Berlet HH (1989) Sensitivity and variability of the Bradford protein assay in the presence of detergents. Anal Biochem 178: 263–268PubMedGoogle Scholar
  51. Gander JE (1984) Gel protein stains: glycoproteins. Methods Enzymol 104: 447–451PubMedGoogle Scholar
  52. Gershoni JM (1988) Protein blotting: a manual. Methods Biochem Anal 33: 1–58PubMedGoogle Scholar
  53. Ghose TK (ed) (1984) Measurement of cellulase activities. Commission on Biotechnology, International Union of Pure and Applied Chemistry, Biochemical Engineering Research Centre, Indian Institute of Technology, New Delhi, IndiaGoogle Scholar
  54. Glenn AR (1976) Production of extracellular proteins by bacteria. Annu Rev Microbiol 30: 41–62PubMedGoogle Scholar
  55. Glenney J (1986) Antibody probing of Western blots which have been stained with indian ink. Anal Biochem 156: 315–319PubMedGoogle Scholar
  56. Glumoff T, Harvey PJ, Molinari S, Goble M, Frank G, Palmer JM, Smit JDG, Leisola MSA (1990) Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes. Eur J Biochem 187: 515–520Google Scholar
  57. Goksoyr J, Eriksen J (1980) Cellulases. In: Rose AH (ed) Microbial enzymes and bioconversions, Economic microbiology, vol 5. Academic Press, New York, pp 283–330Google Scholar
  58. Hahlbrock K, Scheel D (1989) Physiology and molecular biology of phenylpropanoid metabolism. Annu Rev Plant Physiol Plant Mol Biol 40: 347–369Google Scholar
  59. Hames BD, Rickwood D (eds) (1989) Gel electrophoresis of proteins — a practical approach, 2nd edn. IRL Press, OxfordGoogle Scholar
  60. Harris ELV, Angal S (eds) (1989) Protein purification methods — a practical approach. IRL Press, OxfordGoogle Scholar
  61. Heftmann E (ed) (1983) Chromatography. Elsevier, AmsterdamGoogle Scholar
  62. Heimgartner U, Kozulic B, Mosbach K (1989) Polyacrylic polyhydrazides as reagents for detection of glycoproteins. Anal Biochem 181: 182–189PubMedGoogle Scholar
  63. Heslop-Harrison Y, Heslop-Harrison J (1981) The digestive glands of Pinguicula: structure and cytochemistry. Ann Bot 47: 293–319Google Scholar
  64. Heukeshoven J, Dernick R (1988) Improved silver staining procedure for fast staining in PhastSystem development unit. I. Staining of sodium dodecyl sulfate gels. Electophoresis 9: 28–32Google Scholar
  65. Hill HD, Straka JG (1988) Protein determination using bicinchoninic acid in the presence of sulfhydryl reagents. Anal Biochem 170: 203–208PubMedGoogle Scholar
  66. Howe JG, Hershey JWB (1981) A sensitive immunoblotting method for measuring protein synthesis initiation factor levels in lysates of Escherichia coll. J Biol Chem 256: 1283612839Google Scholar
  67. International Union of Biochemistry (1984) Enzyme nomenclature. Academic Press, LondonGoogle Scholar
  68. Janson J-C, Rydén L (eds) (1989) Protein purification — principles, high resolution methods, and application. VCH Publishers, New YorkGoogle Scholar
  69. Jensen HS (1984) Adsorbed soluble [3H]elastin as substrate for proteinase activity. A new microassay technique. Biochem J 218: 645–648PubMedGoogle Scholar
  70. Jones TM, Anderson AJ, Albersheim P (1972) Host-pathogen interactions. IV. Studies on the polysaccharide-degrading enzymes secreted by Fusarium oxysporum f. sp. lycopersici. Physiol Plant Pathol 2: 153–166Google Scholar
  71. Joosten MHAJ, De Wit PJGM (1989) Identification of several pathogenesis-related proteins in tomato leaves inoculated with Cladosporium fulvum (syn Fulvia fulva) as 1,3-f3-glucanases and chitinases. Plant Physiol 89: 945–951PubMedGoogle Scholar
  72. Kalisz HM (1988) Microbial proteinases. Adv Biochem Eng Biotechnol 36: 1–65PubMedGoogle Scholar
  73. Kauffmann S, Legrand M, Geoffroy P, Fritig B (1987) Biological function of pathogenesis- related proteins: four PR proteins of tobacco leaves have 1,3–13-glucanase activity. EMBO J 6: 3209–3212PubMedGoogle Scholar
  74. Keen NT, Dahlbeck D, Staskawicz B, Belser W (1984) Molecular cloning of pectate lyase genes from Erwinia chrysanthemi EC16 and their high level expression in Escherichia coll. J Bacteriol 159: 825–831PubMedGoogle Scholar
  75. Kollatukudy PE (1985) Enzymatic penetration of the plant cuticle by fungal pathogens. Annu Rev Phytopathol 23: 223–250Google Scholar
  76. Kollatukudy PE, Purdy RE, Maiti IB (1981) Cutinases from fungi and pollen. Methods Enzymol 71: 652–664Google Scholar
  77. Kombrik E, Schröder M, Hahlbrock K (1988) Several pathogenesis-related proteins in potato are (3–1,3-glucanases and chitinases. Proc Natl Acad Sci USA 85: 782–786Google Scholar
  78. Künnecke W, Kalisz HM, Schmid RD (1989) Flow injection zymography — a novel procedure for the on-line detection of enzyme activity. Anal Lett 22: 1471–1484Google Scholar
  79. Lamb CJ, Lawton MA, Dron M, Dixon RA (1989) Signals and transduction mechanisms for activation of plant defences against microbial attack. Cell 56: 215–224PubMedGoogle Scholar
  80. Legler G, Müller-Platz CM, Mentges-Hettkamp M, Pflieger G, Jülich E (1985) On the chemical basis of the Lowry protein determination. Anal Biochem 150: 278–287PubMedGoogle Scholar
  81. Legrand M, Kauffmann S, Geoffroy P, Fritig B (1987) Biological function of pathogenesis-related proteins: four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci USA 84: 6750–6754PubMedGoogle Scholar
  82. Lin TS, Kollatukudy PE (1978) Induction of a biopolyester hydrolase (cutinase) by lowGoogle Scholar
  83. levels of cutin monomers in Fusarium solani f. sp. pisi. J Bacteriol 133:942–951 Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with theGoogle Scholar
  84. Folin phenol reagent. J Biol Chem 193:265–275Google Scholar
  85. MacKenzie CR, Williams RE (1984) Detection of cellulase and xylanase activity in isoelectric-focused gels using agar substrate gels supported on plastic film. Can J Microbiol 30: 1522–1525Google Scholar
  86. Maiti IB, Koilatukudy PE (1979) Prevention of fungal infection of plants by specific inhibition of cutinase. Science 205: 507–508PubMedGoogle Scholar
  87. Mauch F, Hadwiger LA, Boller T (1984) Ethylene: symptom, not signal for the induction of chitinase and (3–1,3-glucanase in pea pods by pathogens and elicitors. Plant Physiol 76: 607–611PubMedGoogle Scholar
  88. Mauch F, Hadwiger LA, Boller T (1988a) Antifungal hydrolases in pea tissue. I. Purification and characterisation of two chitinases and two 13–1,3-glucanases differentially regulated during development and in response to fungal infection. Plant Physiol 87: 325–333PubMedGoogle Scholar
  89. Mauch F, Mauch-Mani B, Boller T (1988b) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and ß-1,3-glucanase. Plant Physiol 88: 936–942PubMedGoogle Scholar
  90. McHale AP, Hackett TJ, McHale LM (1989) Specific zymogram staining procedure for the exocellobiohydrolase components produced by Talaromyces emersonii CBS 814.70. Enzyme Microb Technol 11: 17–20Google Scholar
  91. Mellor RB, Mörschel E, Werner D (1984) Legume root response to symbiotic infection: enzymes of the peribacteroid space. Z Naturforsch 39c: 123–125Google Scholar
  92. Miller GL, Blum R, Glennon WE, Burton AL (1960) Measurement of carboxymethylcellulase activity. Anal Biochem 1: 127–132Google Scholar
  93. Munoz G, Marshall S, Cabrera M, Horvat A (1988) Enhanced detection of glycoproteins in polyacrylamide gels. Anal Biochem 170: 491–494PubMedGoogle Scholar
  94. Nakamura K, Tanaka T, Kuwahara A, Takeo K (1985) Microassay for proteins on nitrocellulose filter using dye-staining procedure. Anal Biochem 148: 311–319PubMedGoogle Scholar
  95. North MJ (1982) Comparative biochemistry of the proteinases of eukaryotic microorganisms. Microbiol Rev 46: 308–340PubMedGoogle Scholar
  96. Ohtakara A (1988) Viscosimetric assay for chitinase. Methods Enzymol 161: 426–430Google Scholar
  97. Ostoa-Saloma P, Ramirez J, Perez-Montfort R (1989) Measurement of casein digestion by a fluorometric method. Anal Biochem 176: 239–243PubMedGoogle Scholar
  98. Page MI (ed) (1984) The chemistry of enzyme action. Elsevier, AmsterdamGoogle Scholar
  99. Payne JW (ed) (1980) Microorganisms and nitrogen sources. J Wiley and Sons, LondonGoogle Scholar
  100. Peterson GL (1979) Review of the Folin phenol protein quantitation method of Lowry, Rosebrough, Farr and Randall. Anal Biochem 100: 201–220PubMedGoogle Scholar
  101. Priest FG (1984) Extracellular enzymes. Aspects of microbiology ser 9. Van Nostrand Reinhold (UK) Co Ltd, Berkshire, EnglandGoogle Scholar
  102. Prieur B, Russo-Marie F (1988) An automated western blot analysis using the PhastSystem. Anal Biochem 172: 338–343PubMedGoogle Scholar
  103. Racusen D (1984) Lipid acyl hydrolase of patatin. Can J Bot 62: 1640–1644Google Scholar
  104. Renganathan V, Usha SN, Lindenburg F (1990) Cellobiose-oxidizing enzymes from the lignocellulose-degrading basidomycete Phyanerochaete chrysosporium: interaction with microcrystalline cellulose. Appl Microbiol Biotechnol 32: 609–613Google Scholar
  105. Rexovâ-Benkovâ L, Markovic 0 (1976) Pectic enzymes. Adv Carbohydr Chem Biochem 33: 323–385Google Scholar
  106. Ried JL, Collmer A (1985) Activity stain for rapid characterisation of pectic enzymes in isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gels. Appl Environ Microbiol 50: 615–622PubMedGoogle Scholar
  107. Ried JL, Collmer A (1986) Comparison of pectic enzymes produced by Erwinia chrysanthemi, Erwinia carotovora, subsp. carotovora, and Erwinia carotovora, subsp. atroseptica. Appl Environ Microbiol 52: 305–310PubMedGoogle Scholar
  108. Rinderknecht H, Geokas MC, Silverman P, Haverback BJ (1968) A new sensitive method for the determination of proteolytic activity. Clin Chim Acta 21: 197–203PubMedGoogle Scholar
  109. Roby D, Esquerre-Tugaye M-T (1987) Induction of chitinases and of translatable mRNA for these enzymes in melon plants infected with Colletotrichum lagenarium. Plant Sci 52: 175–185Google Scholar
  110. Rodriguez-Vico F, Martinez-Cayuela M, Garcia-Pergrin E, Ramirez H (1989) A procedure for eliminating interferences in the Lowry method of protein determination. Anal Biochem 183: 275–278PubMedGoogle Scholar
  111. Rohringer R, Holden DW (1985) Protein blotting: detection of proteins with colloidal gold, and of glycoproteins and lectins with biotin-conjugated and enzyme probes. Anal Biochem 144: 118–127PubMedGoogle Scholar
  112. Rombouts FM, Pilnik W (1980) Pectic enzymes. In: Rose AH (ed) Microbial enzymes and bioconversions. Economic microbiology, vol 5. Academic Press, New York, pp 227–282Google Scholar
  113. Root DD, Reisler E (1989) Copper iodide staining of protein blots on nitrocellulose membranes. Anal Biochem 181: 250–253PubMedGoogle Scholar
  114. Ryan CA (1984) Systemic responses to wounding. In: Kosuge T, Nester EW (eds) Plant-microbe interactions, vol 1. Macmillan, New York, pp 307–320Google Scholar
  115. Sacher JA, Tseng J, Williams R, Cabello A (1982) Wound-induced RNAse activity in sweet potato. Plant Physiol 69: 1060–1065PubMedGoogle Scholar
  116. Saddler JN, Khan AW (1981) Cellulolytic enzyme system of Acetivibrio cellulolyticus. Can J Microbiol 27: 288–294PubMedGoogle Scholar
  117. Schlumbaum A, Mauch F, Vögeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365–367Google Scholar
  118. Schwarz WH, Bronnenmeier K, Gräbnitz F, Staudenbauer WL (1987) Activity staining of cellulases in polyacrylamide gels containing mixed linkage 3-glucans. Anal Biochem 164: 72–77PubMedGoogle Scholar
  119. Scopes RK (1987) Protein purification — principles and practise, 2nd edn. Springer Berlin Heidelberg New YorkGoogle Scholar
  120. Segel IH (1975) Enzyme kinetics. Wiley and Sons, New YorkGoogle Scholar
  121. Sexton R, Roberts JA (1982) Cell biology of abscission. Annu Rev Plant Physiol 33: 133–162Google Scholar
  122. Shaykh M, Soliday C, Kolattukudy PE (1977) Proof for the production of cutinase by Fusarium solani f. pisi during penetration into its host, Pisum sativum. Plant Physiol 60: 170–172PubMedGoogle Scholar
  123. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150: 76–85PubMedGoogle Scholar
  124. Solheim B, Fjellheim KE (1984) Rhizobial polysaccharide-degrading enzymes from roots of legumes. Physiol Plant 62: 11–17Google Scholar
  125. Soliday CL, Flurkey WH, Okita TW, Kolattukudy PE (1984) Cloning and structure determination of cDNA for cutinase, an enzyme involved in fungal penetration of plants. Proc Natl Acad Sci USA 81: 3939–3943PubMedGoogle Scholar
  126. Spiro RG (1966) Analysis of sugars found in glycoproteins. Methods Enzymol 8: 3–26Google Scholar
  127. Stoessl A (1983) Secondary plant metabolites in preinfectional and postinfectional resistance. In: Bailey JA, Deverall BJ (eds) The dynamics of host defence. Academic Press, New York, pp 71–122Google Scholar
  128. Suelter CH (1985) A practical guide to enzymology. J Wiley and Sons, New YorkGoogle Scholar
  129. Switzer RC, Merril CR, Shifrin S (1979) A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem 98: 231–237PubMedGoogle Scholar
  130. Tien M, Kirk TK (1988) Lignin peroxidase of Phanerochaete chrysosporium. Methods Enzymol 161: 238–249Google Scholar
  131. Trudel J, Asselin A (1989) Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal Biochem 178: 362–366PubMedGoogle Scholar
  132. Veluthambi K, Mahadevan S, Maheshwari R (1981) Trehalose toxicity in Cuscuta reflexa. Plant Physiol 68: 1369–1374PubMedGoogle Scholar
  133. Vögeli U, Meins F, Boller T (1988) Co-ordinated regulation of chitinase and 3–1,3glucanase in bean leaves. Planta 174: 364–372Google Scholar
  134. Walter H, Brooks DE, Fisher D (eds) (1985) Partitioning in aqueous two-phase systems: theory, methods, uses, and applications in biotechnology. Academic Press, LondonGoogle Scholar
  135. Wargo PM (1975) Lysis of the cell wall of Armillaria mellea by enzymes from forest trees. Physiol Plant Pathol 5: 99–105Google Scholar
  136. Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244: 4406–4412PubMedGoogle Scholar
  137. Westergaard JL, Hackbarth C, Treuhaft MW, Robterts RC (1980) Detection of proteinases in electrophoretograms of complex mixtures. J Immunol Methods 34: 167175Google Scholar
  138. Woloshuk CP, Kollatukudy PE (1986) Mechanism by which contact with plant cuticle triggers cutinase gene expression in the spores of Fusarium solani f. sp. pisi. Proc Natl Acad Sci USA 83: 1704–1708PubMedGoogle Scholar
  139. Wong P, Barbeau A, Roses AD (1985) A method to quantitate Coomassie blue-stained proteins in cylindrical polyacrylamide gels. Anal Biochem 150: 288–293PubMedGoogle Scholar
  140. Wood TM, McCrae SI (1979) Synergism between enzymes involved in the solubilisation of native cellulose. Adv Chem Ser 181: 181–209Google Scholar
  141. Wood WA, Kellogg ST (eds) (1988) Methods in enzymology, vol 160. Academic Press, New YorkGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • H. M. Kalisz
  • M. E. Kalisz

There are no affiliations available

Personalised recommendations