HomeThe Philippine Journal of Biochemistry and Molecular Biology (PJBMB)vol. 2 no. 1 (1979)

Peroxidase Activity and Isozyme PAttern of Different Clones/Varieties of Sugatcane (Saccharum officinarum l.) with varying resistance to smut (caused by Ustilago scitaminea Sydow)

Pamela G. Fernandez | Azucena L. Carpena | Evelyn Mae T. Mendoza

 

Abstract:

The association of peroxidase activity and isozyme pattern with smut resistance in sugarcane was studied. Co 440 (immune), HQ 409 (intermediate resistant), two immune, and two highly susceptible progenies of the two varieties, one resistant control, CAC 57-13, and one susceptible control Phil 56-226, comprise the eight clones investigated. Peroxidase activity was found not to differ significantly among the clones. No significant correlation was observed between peroxidase activity of healthy tissue and healthy part of infected tissue and percent field infection. Infected tissues showed alteration in their isozyme pattern as compared to that of healthy tissues; there was evident increase in peroxidase activity in some isozymes and a decrease in others. However, among the various clones, the isozyme pattern did not show distinct features to differentiate immune/resistant from susceptible clones. The results indicate that peroxidase may not be involved in smut resistance of sugarcane and hence, may not be used as an index for such resistance.



References:

  1. Kedar, N. (1959). Title of article. American Potato Journal, 36, 215–224.
  2. Gretchushnikov, A. I., & Popkova, K. V. (1958). Title of article. Izvestiya Akademii Nauk SSSR. Seriya Biologicheskaya, 4, 456–462.
  3. Siegel, B. Z., & Galston, A. W. (1967). Title of article. Plant Physiology, 42, 221–226.
  4. Turian, G., & Hamilton, R. H. (1960). Title of article. Biochimica et Biophysica Acta, 41, 148–150.
  5. Hoyle, M. C. (1972). Title of article. Plant Physiology, 50, 15–18.
  6. Martin, J. P., Abbott, E. V., & Hughes, C. G. (1961). Sugarcane diseases of the world (Vol. 1). Elsevier Publishing Co.
  7. Flores, C. I. (1978). Title of article. Philippine Journal of Crop Science, 3(2), 121–125.
  8. Worthington Biochemical Corporation. (1972). Worthington enzyme manual: Peroxidase assay (pp. 43–45). Worthington Biochemical Corp.
  9. Lowry, O. H., Rosenbrough, N. V., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.
  10. Davis, B. J. (1964). Disc electrophoresis. II. Method and application to human serum proteins. Annals of the New York Academy of Sciences, 121, 404–427.
  11. Mujer, C. V. (1977). A comparison of the ontogenetic development of peroxidase and catalase isozymes in the makapuno and normal endosperm of the coconut [Unpublished bachelor's thesis]. University of the Philippines at Los Baños.
  12. Work, T. S., & Work, E. (1969). Laboratory techniques in biochemistry and molecular biology (Vol. 1). North-Holland Publishing Company.
  13. Thom, M., & Maretzki, A. (1970). Peroxidase and esterase isozymes in Hawaiian sugarcane. Hawaiian Planters' Record, 58, 81–94.
  14. Goodman, R. N., Kiraly, Z., & Zaitlin, M. (1967). The biochemistry and physiology of infectious plant disease. D. Van Nostrand Co., Inc.
  15. Pryor, A. (1976). Title of article. Physiological Plant Pathology, 8, 307–331.
  16. Shannon, L. M. (1968). Plant isoenzymes. Annual Review of Plant Physiology, 19, 187–210.
  17. Ockerse, R., Siegel, B. Z., & Galston, A. W. (1966). Hormone-induced IAA oxidase in pea stem segments. Science, 151, 452–453.