Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 1,525

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 access
Weydert, Christine J, Cullen, Joseph J·2010·Nature Protocols

Abstract

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nprot.2009.197

Cites

45 of 45 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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

Show all 45 references

Research works printed but not linked: 8

  1. 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).
  2. 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
  3. 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
  4. 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
  5. 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).
  6. 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).
  7. 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).
  8. 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

See all 1,525

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.