The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Stabilization of Adenylate Energy Charge by the Adenylate Deaminase Reaction
Open accessAbstract
Abstract In the physiological range of the adenylate energy charge in liver (0.7 to 0.9) the rate of deamination of AMP catalyzed by rat liver adenylate deaminase (EC 3.5.4.6) increases sharply with decreasing energy charge. It is suggested that this response serves to protect against sharp transient decreases in energy charge: when the charge decreases the resulting removal of AMP by deamination will oppose the decrease in charge (the mole fraction of ATP plus half the mole fraction of ADP). The activity of the enzyme decreases sharply as the size of the adenine nucleotide pool decreases in and below the physiological range. This effect may be a self-limiting response to prevent excessive depletion of the pool. These suggestions, based on the properties of the enzyme observed in vitro, are consistent with the results of experiments on liver in vivo reported by other workers.
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Cites
Energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers
Atkinson, D. E. (1968) · Biochemistry · doi:10.1021/bi00851a033 · Cited by 2,401
Self-citationDIFFERENTIAL SPECTROPHOTOMETRY OF PURINE COMPOUNDS BY MEANS OF SPECIFIC ENZYMES
Kalckar, H. M. (1947) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30999-7 · Cited by 1,118
Adenylate Energy Charge in Escherichia coli During Growth and Starvation
Chapman, A. G., Fall, L., & Atkinson, D. E. (1971) · Journal of Bacteriology · doi:10.1128/jb.108.3.1072-1086.1971 · Cited by 779
Self-citationThe Regulation of Glycolysis and Gluconeogenesis in Animal Tissues
Scrutton, M. C., & Utter, M. F. (1968) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.37.070168.001341 · Cited by 631
The Concentrations of Free and Bound Magnesium in Rat Tissues
Veloso, D., Guynn, R. W., Oskarsson, M., & Veech, R. L. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43738-1 · Cited by 383
Liver Adenine Nucleotides: Fructose-Induced Depletion and Its Effect on Protein Synthesis
Mäenpää, P. H., Raivio, K. O., & Kekomäki, M. P. (1968) · Science · doi:10.1126/science.161.3847.1253 · Cited by 343
Faupel, R. P., Seitz, H. J., Tarnowski, W., Thiemann, V., & Weiss, C. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90170-1 · Cited by 209
Burch, H. B., Lowry, O. H., Meinhardt, L., Max, P., & Chyu, K.-J. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63211-9 · Cited by 202
McComb, R. B., & Yushok, W. D. (1964) · PubMed · Cited by 66
Cited by
O’Brien III, W. G., Berka, V., Tsai, A.-L., Zhao, Z., & Lee, C. C. (2015) · Scientific Reports · doi:10.1038/srep13147 · Cited by 20
Metadata
- Authors
- Chapman, A. G., & Atkinson, D. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1973-12
- Volume
- 248
- Issue
- 23
- Pages
- 8309-8312
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1567446278
- Cited by
- 324
- References
- 9
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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