Abstract
Shoots, roots, and seeds of corn (Zea mays L., cv. Michigan 500), oats (Avena sativa L., cv. Au Sable), and peas (Pisum sativum L., cv. Wando) were analyzed for their superoxide dismutase content using a photochemical assay system consisting of methionine, riboflavin, and p-nitro blue tetrazolium. The enzyme is present in the shoots, roots, and seeds of the three species. On a dry weight basis, shoots contain more enzyme than roots. In seeds, the enzyme is present in both the embryo and the storage tissue. Electrophoresis indicated a total of 10 distinct forms of the enzyme. Corn contained seven of these forms and oats three. Peas contained one of the corn and two of the oat enzymes. Nine of the enzyme activities were eliminated with cyanide treatment suggesting that they may be cupro-zinc enzymes, whereas one was cyanide-resistant and may be a manganese enzyme. Some of the leaf superoxide dismutases were found primarily in mitochondria or chloroplasts. Peroxidases at high concentrations interfere with the assay. In test tube assays of crude extracts from seedlings, the interference was negligible. On gels, however, peroxidases may account for two of the 10 superoxide dismutase forms.
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- Asada K., Urano M., Takahashi M. Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxide dismutase. Eur J Biochem. 1973 Jul 2;36(1):257–266. doi: 10.1111/j.1432-1033.1973.tb02908.x. [DOI] [PubMed] [Google Scholar]
- Beauchamp C. O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim Biophys Acta. 1973 Jul 12;317(1):50–64. doi: 10.1016/0005-2795(73)90198-0. [DOI] [PubMed] [Google Scholar]
- Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
- 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]
- Fridovich I. Oxygen: boon and bane. Am Sci. 1975 Jan-Feb;63(1):54–59. [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]
- Gregory E. M., Yost F. J., Jr, Fridovich I. Superoxide dismutases of Escherichia coli: intracellular localization and functions. J Bacteriol. 1973 Sep;115(3):987–991. doi: 10.1128/jb.115.3.987-991.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Khan A. U. Singlet molecular oxygen from superoxide anion and sensitized fluorescence of organic molecules. Science. 1970 Apr 24;168(3930):476–477. doi: 10.1126/science.168.3930.476. [DOI] [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]
- Lumsden J., Hall D. O. Chloroplast manganese and superoxide. Biochem Biophys Res Commun. 1975 May 19;64(2):595–602. doi: 10.1016/0006-291x(75)90363-0. [DOI] [PubMed] [Google Scholar]
- Lumsden J., Hall D. O. Soluble & membrane-bound superoxide dismutases in a blue-green algae (Spirulina)and spinach. Biochem Biophys Res Commun. 1974 May 7;58(1):35–41. doi: 10.1016/0006-291x(74)90887-0. [DOI] [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]
- Pammenter N. W., Adamson J. H., Berjak P. Viability of stored seed: extension by cathodic protection. Science. 1974 Dec 20;186(4169):1123–1124. doi: 10.1126/science.186.4169.1123. [DOI] [PubMed] [Google Scholar]
- Sawada Y., Oyama T., Yamazaki I. Preparation and physicochemical properties of green pea superoxide dismutase. Biochim Biophys Acta. 1972 May 12;268(2):305–312. doi: 10.1016/0005-2744(72)90325-7. [DOI] [PubMed] [Google Scholar]
- Smillie R. M. Synthesizing capability of the photosynthetic apparatus: proteins. Methods Enzymol. 1972;24:381–394. doi: 10.1016/0076-6879(72)24084-8. [DOI] [PubMed] [Google Scholar]
- Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J Biol Chem. 1973 May 25;248(10):3582–3592. [PubMed] [Google Scholar]