The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue
Open accessAbstract
Cells contain a large number of antioxidants to prevent or repair the damage caused by reactive oxygen species, as well as to regulate redox-sensitive signaling pathways. General protocols are described to measure the antioxidant enzyme activity of superoxide dismutase (SOD), catalase and glutathione peroxidase. The SODs convert superoxide radical into hydrogen peroxide and molecular oxygen, whereas the catalase and peroxidases convert hydrogen peroxide into water. In this way, two toxic species, superoxide radical and hydrogen peroxide, are converted to the harmless product water. Western blots, activity gels and activity assays are various methods used to determine protein and activity in both cells and tissue depending on the amount of protein required for each assay. Other techniques including immunohistochemistry and immunogold can further evaluate the levels of the various antioxidant enzymes in tissues and cells. In general, these assays require 24–48 h to complete.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Aebi, H. (1984) · Methods in Enzymology · doi:10.1016/s0076-6879(84)05016-3 · Cited by 25,696
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 18,892
Burton, K. (1956) · Biochemical Journal · doi:10.1042/bj0620315 · Cited by 14,090
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
Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Paglia, D. E., & Valentine, W. N. (1967) · PubMed · Cited by 10,889
A SPECTROPHOTOMETRIC METHOD FOR MEASURING THE BREAKDOWN OF HYDROGEN PEROXIDE BY CATALASE
Beers, R. F., & Sizer, I. W. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50881-x · Cited by 6,761
DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*
Ornstein, L. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14207.x · Cited by 4,565
Glutathione peroxidase activity in selenium-deficient rat liver
Lawrence, R. A., & Burk, R. F. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90747-6 · Cited by 3,528
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X.-M., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,419
Research works printed but not linked: 8
- Shibanuma, M., Kuroki, T. & Nose, K. Induction of DNA replication and expression of proto-oncogenes c-myc and c-fos in quiescent Balb/3T3 cells by xanthine/xanthine oxidase. Oncogene 3, 17–21 (1988).
- Nishikawa, M., Tamada, A., Kumai, H., Yamashita, F. & Hashida, M. Inhibition of experimental pulmonary metastasis by controlling biodistribution of catalase in mice. Int. J. Cancer 99, 474–479 (2002). · doi:10.1002/ijc.10387
- Kelner, M.J., Bagnell, R.D., Uglik, S.F., Montoya, M.A. & Mullenbach, G.T. Heterologous expression of selenium-dependent glutathione peroxidase afford cellular resistance to paraquat. Arch. Biochem. Biophys. 323, 40–46 (1995). · doi:10.1006/abbi.1995.0007
- Lewis, A. et al. Metastatic progression of pancreatic cancer: changes in antioxidant enzymes and cell growth. Clin. Exp. Metastasis 22, 523–532 (2006). · doi:10.1007/s10585-005-4919-7
- Czaja, M.J. et al. Induction of MnSOD gene expression in a hepatic model of TNF-α toxicity does not result in increased protein. Am. J. Physiol. 266, G737–G744 (1994).
- Treadwell, F.P. & Hall, W.T. Analytical chemistry. In Analytical Chemistry. Based on the German text by F.P. Treadwell edn. 9, Vol. 2 (ed. Hall, W.T.) (John Wiley & Sons, New York, New York, 1948).
- Günzler, W.A. & Flohé, L. Glutathione peroxidase. In Handbook of Methods for Oxygen Radical Research (ed. Greenwald, R.A.) 285–290 (CRC Press, Boca Raton, Florida, 1985).
- Lam, E.W.N. et al. Immunolocalization and adenoviral vector-mediated manganese superoxide dismutase gene transfer to experimental oral tumors. J. Dent. Res. 79, 1410–1417 (2000). · doi:10.1177/00220345000790061001
Cited by
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Xie, N., Zhang, L., Gao, W., Huang, C., Huber, P. E., Zhou, X., Li, C., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,052
Redox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 359
Wang, T., Jian, Z., Baskys, A., Yang, J., Li, J., Guo, H., Hei, Y., Xian, P., He, Z., Li, Z., et al. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120264 · Cited by 266
Oxidative Stress and Antioxidants—A Critical Review on In Vitro Antioxidant Assays
Kotha, R. R., Tareq, F. S., Yildiz, E., & Luthria, D. L. (2022) · Antioxidants · doi:10.3390/antiox11122388 · Cited by 259
Mitochondrial abnormalities in temporal lobe of autistic brain
Tang, G., Gutierrez Rios, P., Kuo, S.-H., Akman, H. O., Rosoklija, G., Tanji, K., Dwork, A., Schon, E. A., DiMauro, S., Goldman, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.006 · Cited by 194
Metadata
- Authors
- Weydert, C. J., & Cullen, J. J.
- Venue
- Nature Protocols
- Published
- 2009-12-17
- Volume
- 5
- Issue
- 1
- Pages
- 51-66
- ISSN
- 1750-2799 (ISSN-L)
- 1754-2189
- OpenAlex
- W1995199032
- Cited by
- 1,525
- References
- 45
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.springer.com/tdm (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue. https://app.cochat.ai/papers/10.1038/nprot.2009.197
- The paper
- Weydert, C. J., & Cullen, J. J. (2010). Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue. Nature Protocols. https://doi.org/10.1038/nprot.2009.197
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.