The DOI matches its Crossref record.
Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase.
Open accessAbstract
Band 3, the anion transport protein of the human erythrocyte, provides the site of association of certain glycolytic enzymes with the membrane. We have now demonstrated that glyceraldehyde-3-P dehydrogenase is inhibited, reversibly and completely, when membrane bound. The inhibition was competitive with respect to NAD+ and arsenate, but was noncompetitive with glyceraldehyde-3-P. Peptide fragments containing the NH2-terminal 23 residues of band 3 also inhibited the enzyme and displaced it from ghosts. Thus, the red cell membrane binding site for glyceraldehyde-3-P dehydrogenase is the same as that for aldolase, the polyanionic NH2-terminal region of the band 3 polypeptide.
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
Cited by
Johnstone, R. M., Adam, M., Hammond, J. R., Orr, L., & Turbide, C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48095-7 · Cited by 2,931
Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
Campanella, M. E., Chu, H., & Low, P. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409741102 · Cited by 406
Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).
Lux, S. E., John, K. M., Kopito, R. R., & Lodish, H. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.23.9089 · Cited by 296
Reversible Post-translational Modification of Proteins by Nitrated Fatty Acids in Vivo
Batthyany, C., Schopfer, F. J., Baker, P. R. S., Durán, R., Baker, L. M. S., Huang, Y., Cerveñansky, C., Branchaud, B. P., & Freeman, B. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602814200 · Cited by 285
Metadata
- Authors
- Tsai, I. H., Murthy, S. N., & Steck, T. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-02
- Volume
- 257
- Issue
- 3
- Pages
- 1438-1442
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1661137134
- Cited by
- 196
- References
- 0
- FWCI
- 14.34
- 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: Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. https://app.cochat.ai/papers/10.1016/s0021-9258(19)68212-8
- The paper
- Tsai, I. H., Murthy, S. N., & Steck, T. L. (1982). Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)68212-8
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.