The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Control of Phosphorylase Activity in a Muscle Glycogen Particle
Open accessAbstract
Abstract A fraction containing a protein-glycogen complex was obtained from rabbit muscle by different procedures involving acid precipitation followed by differential centrifugation, direct differential centrifugation, and acetone fractionation. All three preparations were essentially identical in terms of their physical, chemical, and enzymatic characteristics strongly suggesting that the protein-glycogen complex represents a structural and functional unit of the cell rather than artifacts resulting from a given isolation procedure. Electron micrographs of the isolated fractions showed the presence of glycogen granules together with vesicles arising from fragments of the sarcoplasmic reticulum. Sedimentation velocity patterns obtained in the analytical ultracentrifuge, sucrose gradient centrifugation, and Sepharose 2B gel filtration indicated that the material can be separated into a light (approximately 120 S) and a heavy (approximately 600 S) fraction. The light fraction consists mainly of glycogen particles to which are associated phosphorylase, phosphorylase kinase, and phosphatase among other enzymes. The heavy fraction contains mainly the elements of the sarcoplasmic reticulum characterized by a strong ATPase activity and some lysosomes as indicated by the presence of traces of acid phosphatase and amylase activity. Contamination of the glycogen particles by this latter enzyme resulted in their slow degradation that prevented further purification.
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Cited by
Glycogen and its metabolism: some new developments and old themes
Roach, P. J., Depaoli-Roach, A. A., Hurley, T. D., & Tagliabracci, V. S. (2012) · Biochemical Journal · doi:10.1042/bj20111416 · Cited by 709
The allosteric transition of glycogen phosphorylase
Barford, D., & Johnson, L. N. (1989) · Nature · doi:10.1038/340609a0 · Cited by 294
Skeletal muscle adaptation: training twice every second day vs. training once daily
Hansen, A. K., Fischer, C. P., Plomgaard, P., Andersen, J. L., Saltin, B., & Pedersen, B. K. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00163.2004 · Cited by 286
Role of glycogen concentration and epinephrine on glucose uptake in rat epitrochlearis muscle.
Jensen, J., Aslesen, R., Ivy, J. L., & Brors, O. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.272.4.e649 · Cited by 95
Marchand, I., Tarnopolsky, M., Adamo, K. B., Bourgeois, J. M., Chorneyko, K., & Graham, T. E. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.122457 · Cited by 71
Metadata
- Authors
- Meyer, F., Heilmeyer, L. M. G., Haschke, R. H., & Fischer, E. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1970-12
- Volume
- 245
- Issue
- 24
- Pages
- 6642-6648
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1560575497
- Cited by
- 356
- References
- 30
- FWCI
- 17.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Meyer, F., Heilmeyer, L. M. G., Haschke, R. H., & Fischer, E. H. (1970). Control of Phosphorylase Activity in a Muscle Glycogen Particle. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)62582-7
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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