Abstract
Catalase, glycolate oxidase, and hydroxypyruvate reductase, enzymes which are located in the microbodies of leaves, show different developmental patterns in the shoots of wheat seedlings. Catalase and hydroxypyruvate reductase are already present in the shoots of ungerminated seeds. Glycolate oxidase appears later. All three enzymes develop in the dark, but glycolate oxidase and hydroxypyruvate reductase have only low activities. On exposure of the seedlings to continuous white light (14.8 × 103 ergs cm−2 sec−1), the activity of catalase is doubled, and glycolate oxidase and hydroxypyruvate reductase activities increase by 4- to 7-fold. Under a higher light intensity, the activities of all three enzymes are considerably further increased. The activities of other enzymes (cytochrome oxidase, fumarase, glucose-6-phosphate dehydrogenase) are unchanged or only slightly influenced by light. After transfer of etiolated seedlings to white light, the induced increase of total catalase activity shows a much longer lag-phase than that of glycolate oxidase and hydroxypyruvate reductase. It is concluded that the light-induced increases of the microbody enzymes are due to enzyme synthesis. The light effect on the microbody enzymes is independent of chlorophyll formation or the concomitant development of functional chloroplasts. Short repeated light exposures which do not lead to greening are very effective. High activities of glycolate oxidase and hydroxypyruvate reductase develop in the presence of 3-amino-1,2,4-triazole which blocks chloroplast development. The effect of light is not exerted through induced glycolate formation and appears instead to be photomorphogenetic in character.
In senescing leaves excised from the plants decreases in activity of glycolate oxidase, and hydroxypyruvate reductase follow with some delay the decrease in chlorophyll content. The activity of catalase, however, is maintained at high levels, especially when the detached shoots are kept in light.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bartels P. G., Hyde A. Chloroplast Development in 4-Chloro-5-(dimethylamino)-2-(alpha,alpha,alpha-trifluoro-m-tolyl)-3 (2H)-pyridazinone (Sandoz 6706)-treated Wheat Seedlings: A Pigment, Ultrastructural, and Ultracentrifugal Study. Plant Physiol. 1970 Jun;45(6):807–810. doi: 10.1104/pp.45.6.807. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bartels P. G., Matsuda K., Siegel A., Weier T. E. Chloroplastic ribosome formation: inhibition by 3-amino-1,2,4-triazole. Plant Physiol. 1967 May;42(5):736–741. doi: 10.1104/pp.42.5.736. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beevers H. Glyoxysomes of castor bean endosperm and their relation to gluconeogenesis. Ann N Y Acad Sci. 1969 Dec 19;168(2):313–324. doi: 10.1111/j.1749-6632.1969.tb43118.x. [DOI] [PubMed] [Google Scholar]
- De Duve C., Baudhuin P. Peroxisomes (microbodies and related particles). Physiol Rev. 1966 Apr;46(2):323–357. doi: 10.1152/physrev.1966.46.2.323. [DOI] [PubMed] [Google Scholar]
- Ellis R. J., Macdonald I. R. Specificity of cycloheximide in higher plant systems. Plant Physiol. 1970 Aug;46(2):227–232. doi: 10.1104/pp.46.2.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ellis R. J. [Chloroplast ribosomes: stereospecificity of inhibition by chloramphenicol]. Science. 1969 Jan 31;163(3866):477–478. doi: 10.1126/science.163.3866.477. [DOI] [PubMed] [Google Scholar]
- Eyster H. C. CATALASE ACTIVITY IN CHLOROPLAST PIGMENT DEFICIENT TYPES OF CORN. Plant Physiol. 1950 Oct;25(4):630–638. doi: 10.1104/pp.25.4.630. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feierabend J., Beevers H. Developmental Studies on Microbodies in Wheat Leaves : II. Ontogeny of Particulate Enzyme Associations. Plant Physiol. 1972 Jan;49(1):33–39. doi: 10.1104/pp.49.1.33. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Filner B., Klein A. O. Changes in enzymatic activities in etiolated bean seedling leaves after a brief illumination. Plant Physiol. 1968 Oct;43(10):1587–1596. doi: 10.1104/pp.43.10.1587. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gerhardt B., Beevers H. Influence of sucrose on protein determination by the Lowry procedure. Anal Biochem. 1968 Aug;24(2):337–339. doi: 10.1016/0003-2697(68)90187-5. [DOI] [PubMed] [Google Scholar]
- Haskins F. A. Changes in the Activities of Several Enzymes during Germination and Seedling Development in Corn (Zea mays L.). Plant Physiol. 1955 Jan;30(1):74–78. doi: 10.1104/pp.30.1.74. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Klein A. O. Persistent photoreversibility of leaf development. Plant Physiol. 1969 Jun;44(6):897–902. doi: 10.1104/pp.44.6.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kuczmak M., Tolbert N. E. Glycolic acid oxidase formation in greening leaves. Plant Physiol. 1962 Nov;37(6):729–734. doi: 10.1104/pp.37.6.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- MARGOLIASH E., NOVOGRODSKY A., SCHEJTER A. Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochem J. 1960 Feb;74:339–348. doi: 10.1042/bj0740339. [DOI] [PMC free article] [PubMed] [Google Scholar]
- RACKER E. Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids. Biochim Biophys Acta. 1950 Jan;4(1-3):211–214. doi: 10.1016/0006-3002(50)90026-6. [DOI] [PubMed] [Google Scholar]
- Rocha V., Ting I. P. Tissue distribution of microbody, mitochondrial, and soluble malate dehydrogenase isoenzymes. Plant Physiol. 1970 Nov;46(5):754–756. doi: 10.1104/pp.46.5.754. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TOLBERT N. E., COHAN M. S. Activation of glycolic acid oxidase in plants. J Biol Chem. 1953 Oct;204(2):639–648. [PubMed] [Google Scholar]
- Tolbert N. E., Oeser A., Kisaki T., Hageman R. H., Yamazaki R. K. Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism. J Biol Chem. 1968 Oct 10;243(19):5179–5184. [PubMed] [Google Scholar]
- Tolbert N. E., Oeser A., Yamazaki R. K., Hageman R. H., Kisaki T. A survey of plants for leaf peroxisomes. Plant Physiol. 1969 Jan;44(1):135–147. doi: 10.1104/pp.44.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tolbert N. E., Yamazaki R. K. Leaf peroxisomes and their relation to photorespiration and photosynthesis. Ann N Y Acad Sci. 1969 Dec 19;168(2):325–341. doi: 10.1111/j.1749-6632.1969.tb43119.x. [DOI] [PubMed] [Google Scholar]
- Tolbert N. E., Yamazaki R. K., Oeser A. Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles. J Biol Chem. 1970 Oct 10;245(19):5129–5136. [PubMed] [Google Scholar]
- Yamazaki R. K., Tolbert N. E. Enzymic characterization of leaf peroxisomes. J Biol Chem. 1970 Oct 10;245(19):5137–5144. [PubMed] [Google Scholar]