Abstract
The activity of 10 enzymes separated by acrylamide disc gel electrophoresis of leaf and stem extracts from Dianthus grown under summer and winter conditions was studied. While banding was constant and highly reproducible under each environment, differences between the 3 cultivars and between the tissues were evident. No significant differences in the isozyme patterns of glutamate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, malate dehydrogenase, and catalase were observed between the 2 environments. Loss of activity was observed under winter conditions with amylase and lactate dehydrogenase and loss of certain isozymic components was evident with acid phosphatase and esterase. Prominent changes were observed in peroxidase isozymes, the hardy cultivars developing additional isozymic components under winter conditions. Only minor changes in the total protein banding were seen. The enzymes showed considerable stability in those tissues killed by the freezing conditions.
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- Coleman E. A., Bula R. J., Davis R. L. Electrophoretic and Immunological Comparisons of Soluble Root Proteins of Medicago sativa L. Genotypes in the Cold Hardened and Non-Hardened Condition. Plant Physiol. 1966 Dec;41(10):1681–1685. doi: 10.1104/pp.41.10.1681. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gerloff E. D., Stahmann M. A., Smith D. Soluble proteins in alfalfa roots as related to cold hardiness. Plant Physiol. 1967 Jul;42(7):895–899. doi: 10.1104/pp.42.7.895. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HINMAN R. L., LANG J. PEROXIDASE-CATALYZED OXIDATION OF INDOLE-3-ACETIC ACID. Biochemistry. 1965 Jan;4:144–158. doi: 10.1021/bi00877a023. [DOI] [PubMed] [Google Scholar]
- Mapson L. W., Wardale D. A. Biosynthesis of ethylene. Enzymes involved in its formation from methional. Biochem J. 1968 Apr;107(3):433–442. doi: 10.1042/bj1070433. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McCown B. H., Beck G. E., Hall T. C. Plant leaf and stem proteins. I. Extraction and electrophoretic separation of the basic, water-soluble fraction. Plant Physiol. 1968 Apr;43(4):578–582. doi: 10.1104/pp.43.4.578. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Parker J. Relationships among cold hardiness, water-soluble protein, anthocyanins, & free sugars in Hedera helix L. Plant Physiol. 1962 Nov;37(6):809–813. doi: 10.1104/pp.37.6.809. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rudolph K., Stahmann M. A. Multiple hydrolases in bean leaves (Phaseolus vulgaris L.) and the effect of the halo blight disease caused by Pseudomonas phaseolicola (Burkh.) Dowson. Plant Physiol. 1966 Mar;41(3):389–394. doi: 10.1104/pp.41.3.389. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scandalios J. G. Genetic control of alcohol dehydrogenase isozymes in maize. Biochem Genet. 1967 Jun;1(1):1–9. doi: 10.1007/BF00487731. [DOI] [PubMed] [Google Scholar]
- Siegel S. M., Halpern L. A. Effects of peroxides on permeability and their modification by indoles, vitamin E, and other substances. Plant Physiol. 1965 Sep;40(5):792–796. doi: 10.1104/pp.40.5.792. [DOI] [PMC free article] [PubMed] [Google Scholar]