Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1986 Aug;81(4):1134–1139. doi: 10.1104/pp.81.4.1134

Heterogeneity of Catalase in Maturing and Germinated Cotton Seeds 1

Christine M Kunce 1, Richard N Trelease 1
PMCID: PMC1075498  PMID: 16664956

Abstract

To investigate possible charge and size heterogeneity of catalase (EC 1.11.1.6) in cotton (Gossypium hirsutum L. cv Deltapine 62), extracts of cotyledons from different developmental ages were subjected to nondenaturing polyacrylamide gel electrophoresis and isoelectric focusing. Special precautions (e.g. fresh homogenates, reducing media) were necessary to prevent artefacts due to enzyme modification during extraction and storage. When the gels were stained for enzyme activity, two distinct electrophoretic forms of catalase were resolved in extracts of maturing and mature cotton seeds. In germinated seeds, three additional cathodic forms were detected revealing a total of five electrophoretic variants. In green cotyledons, the two anodic forms characteristic of ungerminated seeds were less active; whereas, the most cathodic form was predominant. All forms of catalase were found in isolated glyoxysomes. Corresponding electrophoretic patterns were found on Western blots probed with anticatalase serum; no immunoreactive, catalytically inactive forms were detected. Western blots of sodium dodecyl sulfate-polyacrylamide gels revealed only one immunoreactive (55 kilodaltons) polypeptide in cotton extracts of all developmental ages. Results from isoelectric focusing and Ferguson plots indicate that the electrophoretic variants of catalase are charge isomers with a molecular weight of approximately 230,000.

Full text

PDF
1136

Images in this article

1136Fig. 1
on p.1136
1136Fig. 2
on p.1136
1136Fig. 3
on p.1136
1138Fig. 6
on p.1138
1138Fig. 7
on p.1138

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Clare D. A., Duong M. N., Darr D., Archibald F., Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem. 1984 Aug 1;140(2):532–537. doi: 10.1016/0003-2697(84)90204-5. [DOI] [PubMed] [Google Scholar]
  2. Crane D., Holmes R. S., Masters C. J. On the relative rates of synthesis and degradation of catalase in vertebrate tissues. Int J Biochem. 1978;9(8):589–596. doi: 10.1016/0020-711x(78)90119-2. [DOI] [PubMed] [Google Scholar]
  3. Crane D., Holmes R., Masters C. Proteolytic modification of mouse liver catalase. Biochem Biophys Res Commun. 1982 Feb 26;104(4):1567–1572. doi: 10.1016/0006-291x(82)91430-9. [DOI] [PubMed] [Google Scholar]
  4. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. FERGUSON K. A. STARCH-GEL ELECTROPHORESIS--APPLICATION TO THE CLASSIFICATION OF PITUITARY PROTEINS AND POLYPEPTIDES. Metabolism. 1964 Oct;13:SUPPL–SUPPL1002. doi: 10.1016/s0026-0495(64)80018-4. [DOI] [PubMed] [Google Scholar]
  6. Fujiki Y., Lazarow P. B. Post-translational import of fatty acyl-CoA oxidase and catalase into peroxisomes of rat liver in vitro. J Biol Chem. 1985 May 10;260(9):5603–5609. [PubMed] [Google Scholar]
  7. Hedrick J. L., Smith A. J. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys. 1968 Jul;126(1):155–164. doi: 10.1016/0003-9861(68)90569-9. [DOI] [PubMed] [Google Scholar]
  8. Holmes R. S., Masters C. J. Epigenetic interconversions of the multiple forms of mouse liver catalase. FEBS Lett. 1970 Nov 9;11(1):45–48. doi: 10.1016/0014-5793(70)80488-4. [DOI] [PubMed] [Google Scholar]
  9. Holmes R. S., Masters C. J. Species specific features of the distribution and multiplicity of mammalian liver catalase. Arch Biochem Biophys. 1972 Jan;148(1):217–223. doi: 10.1016/0003-9861(72)90134-8. [DOI] [PubMed] [Google Scholar]
  10. Jones G. L., Masters C. J. On the nature and characteristics of the multiple forms of catalase in mouse liver. Arch Biochem Biophys. 1975 Jul;169(1):7–21. doi: 10.1016/0003-9861(75)90311-2. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Mainferme F., Wattiaux R. Effect of lysosomes on rat-liver catalase. Eur J Biochem. 1982 Oct;127(2):343–346. doi: 10.1111/j.1432-1033.1982.tb06877.x. [DOI] [PubMed] [Google Scholar]
  13. Mörikofer-Zwez S., Cantz M., Kaufmann H., von Wartburg J. P., Aebi H. Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties. Eur J Biochem. 1969 Nov;11(1):49–57. doi: 10.1111/j.1432-1033.1969.tb00737.x. [DOI] [PubMed] [Google Scholar]
  14. Robbi M., Lazarow P. B. Synthesis of catalase in two cell-free protein-synthesizing systems and in rat liver. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4344–4348. doi: 10.1073/pnas.75.9.4344. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Schiefer S., Teifel W., Kindl H. Plant microbody proteins, I. Purification and characterization of catalase from leaves of lens culinaris. Hoppe Seylers Z Physiol Chem. 1976 Feb;357(2):163–175. doi: 10.1515/bchm2.1976.357.1.163. [DOI] [PubMed] [Google Scholar]
  16. Trelease R. N., Becker W. M., Gruber P. J., Newcomb E. H. Microbodies (Glyoxysomes and Peroxisomes) in Cucumber Cotyledons: Correlative Biochemical and Ultrastructural Study in Light- and Dark-grown Seedlings. Plant Physiol. 1971 Oct;48(4):461–475. doi: 10.1104/pp.48.4.461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tsaftaris A. S., Scandalios J. G. The multi-locus catalase gene-enzyme system of maize: a model system for the study of gene regulation and enzyme differentiation and function in higher plants. Isozymes Curr Top Biol Med Res. 1983;7:59–77. [PubMed] [Google Scholar]
  18. Yamaguchi J., Nishimura M., Akazawa T. Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4809–4813. doi: 10.1073/pnas.81.15.4809. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES