The DOI matches its Crossref record.
Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct.
Open accessAbstract
We have examined the question, is the carbohydrate moiety of ovalbumin attached to nascent chains or to the completed protein after its release from polyribosomes. Ovalbumin nascent chains have been isolated from hen oviduct by immunoprecipitation of ovalbumin-synthesizing polysomes and subsequent isolation of peptidyl-tRNA by DEAE-cellulose chromatography. Our results indicate that both glucosamine and mannose are incorporated into ovalbumin nascent chains by hen oviduct fragments. Although the asparagine to which the carbohydrates are attached is 10 amino acid residues from the NH2 terminus, the majority of the carbohydrate, if not all, is attached only to those peptide chains that have been essentially completed.
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
INHIBITORS OF THE BIOSYNTHESIS AND PROCESSING OF N-LINKED OLIGOSACCHARIDE CHAINS
Elbein, A. D. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.002433 · Cited by 1,122
The complete amino-acid sequence of hen ovalbumin
NISBET, A. D., SAUNDRY, R. H., MOIR, A. J. G., FOTHERGILL, L. A., & FOTHERGILL, J. E. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05243.x · Cited by 470
Influence of the Carbohydrate Moiety on the Stability of Glycoproteins
Wang, C., Eufemi, M., Turano, C., & Giartosio, A. (1996) · Biochemistry · doi:10.1021/bi9517704 · Cited by 344
Metadata
- Authors
- Kiely, M. L., McKnight, G. S., & Schimke, R. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1976-09
- Volume
- 251
- Issue
- 18
- Pages
- 5490-5495
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584590512
- Cited by
- 217
- References
- 0
- FWCI
- 13.25
- 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: Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct. https://app.cochat.ai/papers/10.1016/s0021-9258(17)33086-7
- The paper
- Kiely, M. L., McKnight, G. S., & Schimke, R. T. (1976). Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)33086-7
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.
