Cited by 895Metal-Catalyzed Oxygenation MechanismsGlutathione Transferases and PolymorphismsRedox biology and oxidative stress

The DOI matches its Crossref record, with a small difference in title or year; 38 of the 38 references it cites were found in a registry or an index.

Superoxide Dismutase

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Weisiger, Richard A., Fridovich, Irwin·1973·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)43969-0

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Abstract

Abstract Fresh chicken liver contains two types of superoxide dismutase, one of which is localized in the mitochondria while the other is found in the cytosol. The mitochondrial superoxide dismutase was inactivated by treatment with mixtures of chloroform and ethanol whereas the cytosol superoxide dismutase was not. The cytosol superoxide dismutase was inhibited by cyanide, whereas the mitochondrial enzyme was not. The cytosol superoxide dismutase was purified to homogeneity and was found to contain copper and zinc and to be similar to the other cupro-zinc superoxide dismutases which have been isolated from diverse eukaryotes. In contrast, the superoxide dismutase present in chicken liver mitochondria, when isolated, was found to a manganoprotein which has a molecular weight of 80,000. It is composed of four subunits of equal size, which are not covalently joined. It contains 2.3 atoms of manganese per molecule and is strikingly similar to the superoxide dismutase previously isolated from bacteria (Keele, B. B., Jr., McCord, J. M., and Fridovich, I. (1970) J. Biol. Chem. 245, 6176–6181; Vance, P. G., Keele, B. B., Jr., and Rajagopalan, K. V. (1972) J. Biol. Chem. 247, 4782–4786). Avimanganin which was isolated from chicken liver mitochondria (Scrutton, M. C. (1971) Biochemistry 10, 3897–3905) appears to be an inactive form of mitochondrial superoxide dismutase. The similarity between the mitochondrial superoxide dismutase and the corresponding enzymes from Escherichia coli and from Streptococcus mutans and the marked dissimilarity to the superoxide dismutase found in the cytosols of eukaryotes lends support to the theory that mitochondria have evolved from aerobic prokaryotes, which entered into an endocellular symbiosis with a protoeukaryote. Chicken liver was not unique in possessing distinct superoxide dismutases in cytosol and in mitochondrial compartments, since the same situation was shown to occur in pig heart. The chicken liver cytosol superoxide dismutase exhibited two peculiar properties. Thus when stored in deep, concentrated solutions it underwent autoreduction to a yellow cuprous form which retained enzymatic activity, and it polymerized to forms which likewise retained activity. Both of these changes were reversible and appeared to be due to reactive sulfhydryl groups which could act as the endogenous reductant and could form intermolecular disulfide bridges. The cytosol superoxide dismutase consisted of a family of electrophoretically distinct forms which could readily be separated on a preparative scale by isoelectric focusing. These multiple forms were indistinguishable in size and in specific activity. The chemical basis of these differences in charge was not explored.

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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129
Superoxide Dismutase
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citation
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citation
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438
Equilibrium Ultracentrifugation of Dilute Solutions*
Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,386
High resolution acrylamide gel electrophoresis of histones
Panyim, S., & Chalkley, R. G. (1969) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(69)90042-3 · Cited by 2,459
THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID
Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,862
ORIGIN OF EUKARYOTIC CELLS
Raven, P. H., & Margulis, L. (1971) · Evolution · doi:10.1111/j.1558-5646.1971.tb01930.x · Cited by 1,483
An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase
McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 976
Self-citation

Show all 37 references

Research works printed but not linked: 4

Tsuchihashi, 1923, Biochem. Z., 140, 63
Cohen, 1970, Amer. Sci., 58, 281
Schnepf, 1972, 2, 299
Dixon, 1935, Proc. Roy. Soc. Ser. B Biol. Sci., 119, 159

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Authors: Weisiger, R. A., & Fridovich, I.
Affiliations: Duke Medical Center (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1973-05
Volume: 248
Issue: 10
Pages: 3582-3592
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)43969-0
OpenAlex: W1580575515
Cited by: 895
References: 37
Citations by year: 2026: 4 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 11 · 2021: 19 · 2020: 20 · 2019: 18 · 2018: 15 · 2017: 13 · 2016: 9 · 2015: 12 · 2014: 25 · 2013: 13 · 2012: 23
FWCI: 35.05
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 17333 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: superoxide dismutase, chicken liver, mitochondrial superoxide dismutase, cytosolic superoxide dismutase, manganese superoxide dismutase, copper-zinc superoxide dismutase, enzyme purification, enzyme inactivation, cyanide inhibition, endosymbiotic origin of mitochondria, autoreduction, porcine heart
MeSH terms: Amino Acids, Animals, Chickens, Copper, Cytoplasm, Cytosol, Electrophoresis, Disc, Isoelectric Focusing, Liver, Manganese, Mitochondria, Liver, Molecular Weight, Myocardium, Oxidation-Reduction, Oxidoreductases, Species Specificity, Superoxide Dismutase, Swine, Ultracentrifugation, Zinc

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