Planta

, Volume 159, Issue 6, pp 505–511

The isolation and characterisation of a catalase-deficient mutant of barley (Hordeum vulgare L.)

  • Alan C. Kendall
  • Alfred J. Keys
  • Janice C. Turner
  • Peter J. Lea
  • Benjamin J. Miflin
Article

DOI: 10.1007/BF00409139

Cite this article as:
Kendall, A.C., Keys, A.J., Turner, J.C. et al. Planta (1983) 159: 505. doi:10.1007/BF00409139

Abstract

A mutant line of barley, R(othamsted)-Pr 79/4, has been isolated which grows poorly in natural air, but normally in air enriched to 0.2% CO2. Analysis of the products of 14CO2 fixation showed that there was no major block in photosynthetic or photorespiratory carbon metabolism in the mutant and that rates of CO2 fixation were only slightly lower than those measured in the wild type (c.v. Maris Mink). Leaves of the mutant line contained only 10% of the catalase (EC 1.11.1.6) activity found in the wild type; and the two major bands of catalase activity detected after starch-gel electrophoresis of extracts of normal leaves were missing from similar extracts of RPr 79/4. Peroxisomes isolated from mutant leaves contained negligible catalase activity, but normal levels of other enzymes involved in photorespiration. Genetic analysis has shown that the mutation is recessive and that both air-sensitivity and catalase-deficiency segregate together in F2 plants derived from a cross between the mutant and the cultivar Golden Promise. [1-14C]Glycollate was not converted to 14CO2 faster in the mutant leaves than in the normal leaves. Thus there was no evidence that photorespiratory CO2 may be obtained by the chemical action of H2O2 on glyoxylate or hydroxypyruvate.

Key words

Catalase deficiencyHordeum (mutant)Mutant (barley)Photorespiration

Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • Alan C. Kendall
    • 1
  • Alfred J. Keys
    • 1
  • Janice C. Turner
    • 1
  • Peter J. Lea
    • 1
  • Benjamin J. Miflin
    • 1
  1. 1.Department of BiochemistryRothamsted Experimental StationHarpendenUK