Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems
The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the mod...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1967 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Theoretical Biology - Amsterdam : Elsevier, 15(1967), 1, Seite 145-176 |
| Übergeordnetes Werk: |
volume:15 ; year:1967 ; number:1 ; pages:145-176 |
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| 245 | 1 | 0 | |a Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems |
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| 520 | |a The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. | ||
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(DE-627)NLEJ183160002 (DE-599)GBVNLZ183160002 DE-627 ger DE-627 rakwb eng Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Semenza, G. oth in Journal of Theoretical Biology Amsterdam : Elsevier 15(1967), 1, Seite 145-176 (DE-627)NLEJ176864393 (DE-600)1470953-3 0022-5193 nnns volume:15 year:1967 number:1 pages:145-176 http://dx.doi.org/10.1016/0022-5193(67)90047-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 15 1967 1 145-176 |
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(DE-627)NLEJ183160002 (DE-599)GBVNLZ183160002 DE-627 ger DE-627 rakwb eng Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Semenza, G. oth in Journal of Theoretical Biology Amsterdam : Elsevier 15(1967), 1, Seite 145-176 (DE-627)NLEJ176864393 (DE-600)1470953-3 0022-5193 nnns volume:15 year:1967 number:1 pages:145-176 http://dx.doi.org/10.1016/0022-5193(67)90047-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 15 1967 1 145-176 |
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(DE-627)NLEJ183160002 (DE-599)GBVNLZ183160002 DE-627 ger DE-627 rakwb eng Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Semenza, G. oth in Journal of Theoretical Biology Amsterdam : Elsevier 15(1967), 1, Seite 145-176 (DE-627)NLEJ176864393 (DE-600)1470953-3 0022-5193 nnns volume:15 year:1967 number:1 pages:145-176 http://dx.doi.org/10.1016/0022-5193(67)90047-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 15 1967 1 145-176 |
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(DE-627)NLEJ183160002 (DE-599)GBVNLZ183160002 DE-627 ger DE-627 rakwb eng Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Semenza, G. oth in Journal of Theoretical Biology Amsterdam : Elsevier 15(1967), 1, Seite 145-176 (DE-627)NLEJ176864393 (DE-600)1470953-3 0022-5193 nnns volume:15 year:1967 number:1 pages:145-176 http://dx.doi.org/10.1016/0022-5193(67)90047-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 15 1967 1 145-176 |
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(DE-627)NLEJ183160002 (DE-599)GBVNLZ183160002 DE-627 ger DE-627 rakwb eng Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Semenza, G. oth in Journal of Theoretical Biology Amsterdam : Elsevier 15(1967), 1, Seite 145-176 (DE-627)NLEJ176864393 (DE-600)1470953-3 0022-5193 nnns volume:15 year:1967 number:1 pages:145-176 http://dx.doi.org/10.1016/0022-5193(67)90047-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 15 1967 1 145-176 |
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rate equations of some cases of enzyme inhibition and activation-their application to sodium-activated membrane transport systems |
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Rate equations of some cases of enzyme inhibition and activation-Their application to sodium-activated membrane transport systems |
| abstract |
The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. |
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The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. |
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The rate equations reported in the present paper refer to the rapid equilibrium kinetics of the following two models: (1) one substrate, two modifiers competing for the same modifier site; (2) one modifier, two substrates competing for the same substrate site.Cases have been considered where the modifier(s) do or do not affect the apparent affinity of the enzyme for the substrate(s); where the modifier(s) do or do not affect the maximal velocity; where compulsory paths in the formation of the enzyme-substrate-modifier compound have to be followed.The equations have been adapted to fit special experimental arrangements, such as constant total concentration of modifiers or, respectively, constant total concentration of substrates.Some equations have been applied to recalculate several data of the literature on sodium-dependent transport system.The good fit of the data with equations derived for the tertiary carrier-substrate-activator model strongly supports Crane's hypothesis on sodium-dependent transport systems. |
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