The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
The effects of glucose and of potassium ions on the interconversion of the two forms of glycogen phosphorylase and of glycogen synthetase in isolated rat liver preparations
Open accessAbstract
1. In the isolated perfused rat liver, increasing glucose concentration from 5.5 to 55 mm in the perfusion medium caused a sequential inactivation of glycogen phosphorylase and activation of glycogen synthetase. The latter change was preceded by a lag period which corresponded to the time required to inactivate the major part of the phosphorylase. 2. The same sequence of events was observed in isolated rat hepatocytes incubated at 37°C. In this preparation, the rate of phosphorylase inactivation was greatly increased by increasing the concentration of glucose and/or of K+ ions in the external medium. The same agents also caused the activation of glycogen synthetase, but this effect was secondary to the inactivation of phosphorylase. 3. In both types of preparations, the rate of synthetase activation was modulated by the residual amount of phosphorylase a that remained after the initial phase of rapid inactivation and was independent of glucose concentration. 4. In isolated hepatocytes, the rate of conversion of glucose into glycogen was propotional to the activity of synthetase a in the preparation. This conversion was preceded by a lag period which could be shortened by increasing either glucose or K+ concentration in the medium. The incorporation of labelled glucose into glycogen was simultaneous with a glycogenolytic process which could not be attributed to the activity of phosphorylase a.
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
HIGH-YIELD PREPARATION OF ISOLATED RAT LIVER PARENCHYMAL CELLS
Berry, M. N., & Friend, D. S. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.43.3.506 · Cited by 4,424
Patterson, M. S., & Greene, R. C. (1965) · Analytical Chemistry · doi:10.1021/ac60226a017 · Cited by 1,454
Thomas, J. A., Schlender, K. K., & Larner, J. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90127-9 · Cited by 1,199
Gluconeogenesis in the perfused rat liver
Hems, R., Ross, B., Berry, M., & Krebs, H. (1966) · Biochemical Journal · doi:10.1042/bj1010284 · Cited by 719
[A simple technic for extremely rapid freezing of large pieces of tissue].
WOLLENBERGER, A., Ristau, O., & Schoffa, G. (1960) · PubMed · Cited by 483
STALMANS, W., & HERS, H. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb04144.x · Cited by 308
Self-citationRate control of the tricarboxylic acid cycle
Krebs, H. A. (1970) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(70)90028-2 · Cited by 196
Wulf, H., Stalmans, W., & Hers, H.-G. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00967.x · Cited by 177
Self-citationEffect of insulin on potassium transfer in isolated rat liver
Mortimore, G. E. (1961) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1961.200.6.1315 · Cited by 176
Cited by
Moore, M., Thor, H., Moore, G., Nelson, S., Moldéus, P., & Orrenius, S. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38834-8 · Cited by 410
Di Monte, D., Bellomo, G., Thor, H., Nicotera, P., & Orrenius, S. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90207-8 · Cited by 375
Hutson, N. J., Brumley, F. T., Assimacopoulos, F. D., Harper, S. C., & Exton, J. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33147-2 · Cited by 348
Keppens, S., Vandenheede, J. R., & De Wulf, H. (1977) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(77)90327-0 · Cited by 305
Hormonal control of pyruvate kinase activity and of gluconeogenesis in isolated hepatocytes.
Feliú, J. E., Hue, L., & Hers, H. G. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.8.2762 · Cited by 220
Self-citation
Metadata
- Authors
- Hue, L., Bontemps, F., & Hers, H.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1975-10-01
- Volume
- 152
- Issue
- 1
- Pages
- 105-114
- ISSN
- 0264-6021 (ISSN-L)
- OpenAlex
- W1839389740
- Cited by
- 356
- References
- 24
- FWCI
- 17.28
- Type
- journal article
- Language
- en
- Open access
- bronze
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: The effects of glucose and of potassium ions on the interconversion of the two forms of glycogen phosphorylase and of glycogen synthetase in isolated rat liver preparations. https://app.cochat.ai/papers/10.1042/bj1520105
- The paper
- Hue, L., Bontemps, F., & Hers, H. (1975). The effects of glucose and of potassium ions on the interconversion of the two forms of glycogen phosphorylase and of glycogen synthetase in isolated rat liver preparations. Biochemical Journal. https://doi.org/10.1042/bj1520105
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.