The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Bovine Erythrocyte Superoxide Dismutase
Open accessAbstract
Abstract The complete primary structure of reduced and S-carboxy-methylated bovine erythrocyte superoxide dismutase has been derived through analysis of peptides from peptic, plasmin, and hydroxylamine digests of the intact polypeptide chain, and from chymotryptic, subtilisin, and dilute acid digests of derived peptides. From these data, the following unique amino acid sequence of 151 residues was deduced, corresponding to a molecular weight of 15,600, in each of the 2 apparently identical subunits of the protein molecule. (Cmc denotes S-carboxymethylcysteine.) [see PDF for equation]
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
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
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43969-0 · Cited by 895
Cited by
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Progressive sequence alignment as a prerequisitetto correct phylogenetic trees
Feng, D.-F., & Doolittle, R. F. (1987) · Journal of Molecular Evolution · doi:10.1007/bf02603120 · Cited by 1,883
Brown, J. L., & Roberts, W. K. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33793-6 · Cited by 270
Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
Cudd, A., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33779-7 · Cited by 211
Metadata
- Authors
- Steinman, H. M., Naik, V. R., Abernethy, J. L., & Hill, R. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1974-11
- Volume
- 249
- Issue
- 22
- Pages
- 7326-7338
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1898798642
- Cited by
- 219
- References
- 2
- FWCI
- 13.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Bovine Erythrocyte Superoxide Dismutase. https://app.cochat.ai/papers/10.1016/s0021-9258(19)42108-x
- The paper
- Steinman, H. M., Naik, V. R., Abernethy, J. L., & Hill, R. L. (1974). Bovine Erythrocyte Superoxide Dismutase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)42108-x
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.