Abstract
The perennating organ, the rhizome, was chosen for examination of response to anoxia in the species Iris pseudacorus L., Iris germanica L. var Quechei, and Glyceria maxima (Hartm.) Holmberg. These monocots are known to differ in their tolerance of anoxia. Intact rhizomes were subjected to periods of prolonged anoxia of up to 28 days and superoxide dismutase (SOD) activity was determined in a 48 hour postanoxic recovery phase. Tests were performed to ensure the accuracy of the measured enzyme activities. In the most anoxia tolerant species, I. pseudacorus, SOD activity rose continuously during the period of imposed anoxia, and levels were maintained in the postanoxic recovery phases: 28 days brought about a 13-fold increase to 1576 U SOD per milligram protein. Small increases were found in the less anoxia tolerant I. germanica during anoxic/postanoxic phases, while a drop in activity was recorded in the least anoxia tolerant G. maxima. However, initial levels in G. maxima were more than twice as high as in the other two species. Experiments applying cycloheximide to anoxic rhizome slices of I. pseudacorus inhibited the increase in SOD activity. This indicates that SOD is, paradoxically, induced under anoxia and we suggest that in this species SOD is one of the enzymes identified as anaerobic polypeptides. The significance of the induction of an `oxygen-protecting' enzyme during complete oxygen deprivation is discussed with regard to a possible critical role during recovery from anoxic stress.
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Selected References
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- Bridges S. M., Salin M. L. Distribution of iron-containing superoxide dismutase in vascular plants. Plant Physiol. 1981 Aug;68(2):275–278. doi: 10.1104/pp.68.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Flohé L., Otting F. Superoxide dismutase assays. Methods Enzymol. 1984;105:93–104. doi: 10.1016/s0076-6879(84)05013-8. [DOI] [PubMed] [Google Scholar]
- Flores R. A rapid and reproducible assay for quantitative estimation of proteins using bromophenol blue. Anal Biochem. 1978 Aug 1;88(2):605–611. doi: 10.1016/0003-2697(78)90462-1. [DOI] [PubMed] [Google Scholar]
- Fridovich I. Superoxide dismutases. Adv Enzymol Relat Areas Mol Biol. 1974;41(0):35–97. doi: 10.1002/9780470122860.ch2. [DOI] [PubMed] [Google Scholar]
- Giannopolitis C. N., Ries S. K. Superoxide dismutases: I. Occurrence in higher plants. Plant Physiol. 1977 Feb;59(2):309–314. doi: 10.1104/pp.59.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUNTER C. S. Pulmonary eosinophilia; report of a case. Br J Tuberc Dis Chest. 1957 Apr;51(2):131–133. doi: 10.1016/s0366-0869(57)80026-4. [DOI] [PubMed] [Google Scholar]
- Haglund U., Lundgren O. Intestinal ischemia and shock factors. Fed Proc. 1978 Nov;37(13):2729–2733. [PubMed] [Google Scholar]
- Halliwell B., Gutteridge J. M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 1984 Apr 1;219(1):1–14. doi: 10.1042/bj2190001. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
- Meerson F. Z., Kagan V. E., Kozlov YuP, Belkina L. M., Arkhipenko YuV The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart. Basic Res Cardiol. 1982 Sep-Oct;77(5):465–485. doi: 10.1007/BF01907940. [DOI] [PubMed] [Google Scholar]
- Mocquot B., Prat C., Mouches C., Pradet A. Effect of anoxia on energy charge and protein synthesis in rice embryo. Plant Physiol. 1981 Sep;68(3):636–640. doi: 10.1104/pp.68.3.636. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pauls K. P., Thompson J. E. In vitro simulation of senescence-related membrane damage by ozone-induced lipid peroxidation. Nature. 1980 Jan 31;283(5746):504–506. doi: 10.1038/283504a0. [DOI] [PubMed] [Google Scholar]
- Peterson G. L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem. 1977 Dec;83(2):346–356. doi: 10.1016/0003-2697(77)90043-4. [DOI] [PubMed] [Google Scholar]
- Quinn P. J., Williams W. P. Plant lipids and their role in membrane function. Prog Biophys Mol Biol. 1978;34(2):109–173. doi: 10.1016/0079-6107(79)90016-6. [DOI] [PubMed] [Google Scholar]