The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
CRYSTALLINE MUSCLE PHOSPHORYLASE
Open accessAbstract
It has been shown that glycogen is a highly branched molecule and that a 1: 6 glucosidic linkage is present at the point of branching (1). Recent fractionation studies of natural starches have shown that two components can be separated (24). One (which is called amylopectin by Meyer (5)) has a branched structure and is similar to glycogen; the other, amylose, is made up of long, unbranched chains of glucose residues in 1:4 glucosidic linkage. Potato starch and corn-starch contain about 20 per cent amylose, the remainder being amylopectin. The polysaccharides formed in vitro by brain, heart, and liver phosphorylase preparations give a brown color with iodine and resemble glycogen (6), while those formed by potato (7) and by muscle phosphorylase (8) have been shown to possess an unbranched structure and to resemble closely the amylose fraction of natural starch. If one assumes that muscle phosphorylase differs from the phosphorylases of other tissues, the fact that muscle contains glycogen and not amylose cannot be explained. Another possibility is to assume that all phosphorylases are of the type of the muscle enzyme; i.e., that they can only form polysaccharides with 1:4 linkages and that another enzyme (or factor) is necessary to make the 1: 6 linkages at the point of branching. The latter enzyme would be present in relatively high concentration in heart, liver, and brain extracts, while muscle extract (for an unknown reason) would contain very little of it.1 Attempts to free liver or heart phosphorylase of the second enzyme have not been successful. The best heart phosphorylase preparations had a purity level of only 20 per cent, if one assumes that pure muscle and heart
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
The reversible formation of starch from glucose-1- phosphate catalysed by potato phosphorylase
Hanes, C. S. (1940) · Proceedings of the Royal Society of London. Series B - Biological Sciences · doi:10.1098/rspb.1940.0035 · Cited by 195
THE KINETICS OF THE ENZYMATIC SYNTHESIS OF GLYCOGEN FROM GLUCOSE-1-PHOSPHATE
Cori, G. T., & Cori, C. F. (1940) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73136-0 · Cited by 173
Self-citationSTARCH PHOSPHORYLASE OF POTATO
Green, D. E., & Stumpf, P. K. (1942) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)72730-0 · Cited by 125
The Synthesis of a Polysaccharide from Glucose-1-Phosphate in Muscle Extract
Cori, C. F., Schmidt, G., & Cori, G. T. (1939) · Science · doi:10.1126/science.89.2316.464 · Cited by 91
Self-citationTHE ACTIVATING EFFECT OF GLYCOGEN ON THE ENZYMATIC SYNTHESIS OF GLYCOGEN FROM GLUCOSE-1-PHOSPHATE
Cori, G. T., & Cori, C. F. (1939) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73512-6 · Cited by 75
Self-citation
Cited by
Serine/threonine phosphatases: mechanism through structure
Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488
The Sulfur Chemistry of Proteins
Cecil, R., & Mcphee, J. R. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60613-0 · Cited by 316
THE MUSCLE PHOSPHORYLASE b KINASE REACTION
Krebs, E. G., Kent, A. B., & Fischer, E. H. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77286-x · Cited by 283
Architecture and activation of human muscle phosphorylase kinase
Yang, X., Zhu, M., Lu, X., Wang, Y., & Xiao, J. (2024) · Nature Communications · doi:10.1038/s41467-024-47049-2 · Cited by 4
Metadata
- Authors
- Green, A. A., & Cori, G. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1943-11
- Volume
- 151
- Issue
- 1
- Pages
- 21-29
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1548175159
- Cited by
- 314
- References
- 5
- FWCI
- 14.01
- 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: CRYSTALLINE MUSCLE PHOSPHORYLASE. https://app.cochat.ai/papers/10.1016/s0021-9258(18)72110-8
- The paper
- Green, A. A., & Cori, G. T. (1943). CRYSTALLINE MUSCLE PHOSPHORYLASE. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)72110-8
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.