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KINETIC ANALYSIS OF ENZYME REACTIONS
Open accessAbstract
Muscle pyruvic phosphoferase,l catalyzing the reaction PEPA + ADP a pyruvate + ATP,2 has been shown to require both Mg+ (3) and K+ or NHb+ ions (4-6) for maximum activity and to be strongly inhibited by Ca+f (4, 5).The mechanism of action of these ions is not known.The principal objective of the research reported in this paper was to acquire information about the activation by K+ ions through the application of kinetic studies.Recent extensions of the theory of enzyme inhibition and activation (7) serve as a basis for the experimental approach applied in this paper.A second objective of this research was to determine whether the activation of rabbit muscle pyruvic phosphoferase was essential or only stimulatory.In previous work (4, 5) the possible indispensable requirement of K+ for rat muscle pyruvic phosphoferase was left open to question.
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Citations
Cited by
Suelter, C. H. (1970) · Science · doi:10.1126/science.168.3933.789 · Cited by 417
The Hormonal Control of Hepatic Gluconeogenesis
EXTON, J. H., MALLETTE, L. E., JEFFERSON, L. S., WONG, E. H. A., FRIEDMANN, N., MILLER, T. B., & PARK, C. R. (1970) · Proceedings of the 1969 Laurentian Hormone Conference · doi:10.1016/b978-0-12-571126-5.50014-5 · Cited by 222
Molecular Mechanisms of Enzyme Activation by Monovalent Cations
Gohara, D. W., & Di Cera, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.737833 · Cited by 97
Metadata
- Authors
- Kachmar, J. F., & Boyer, P. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1953-02
- Volume
- 200
- Issue
- 2
- Pages
- 669-682
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W105375935
- Cited by
- 365
- References
- 0
- FWCI
- 23.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: KINETIC ANALYSIS OF ENZYME REACTIONS. https://app.cochat.ai/papers/10.1016/s0021-9258(18)71413-0
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- Kachmar, J. F., & Boyer, P. D. (1953). KINETIC ANALYSIS OF ENZYME REACTIONS. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)71413-0
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