Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex
The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature i...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1975 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 64(1975), 3, Seite 797-802 |
| Übergeordnetes Werk: |
volume:64 ; year:1975 ; number:3 ; pages:797-802 |
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NLEJ184200164 |
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| 245 | 1 | 0 | |a Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex |
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| 520 | |a The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. | ||
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| 700 | 1 | |a Ward, R.L. |4 oth | |
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(DE-627)NLEJ184200164 (DE-599)GBVNLZ184200164 DE-627 ger DE-627 rakwb eng Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Larry Cottam, G. oth Ward, R.L. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 64(1975), 3, Seite 797-802 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:64 year:1975 number:3 pages:797-802 http://dx.doi.org/10.1016/0006-291X(75)90117-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 64 1975 3 797-802 |
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(DE-627)NLEJ184200164 (DE-599)GBVNLZ184200164 DE-627 ger DE-627 rakwb eng Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Larry Cottam, G. oth Ward, R.L. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 64(1975), 3, Seite 797-802 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:64 year:1975 number:3 pages:797-802 http://dx.doi.org/10.1016/0006-291X(75)90117-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 64 1975 3 797-802 |
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(DE-627)NLEJ184200164 (DE-599)GBVNLZ184200164 DE-627 ger DE-627 rakwb eng Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Larry Cottam, G. oth Ward, R.L. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 64(1975), 3, Seite 797-802 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:64 year:1975 number:3 pages:797-802 http://dx.doi.org/10.1016/0006-291X(75)90117-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 64 1975 3 797-802 |
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(DE-627)NLEJ184200164 (DE-599)GBVNLZ184200164 DE-627 ger DE-627 rakwb eng Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Larry Cottam, G. oth Ward, R.L. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 64(1975), 3, Seite 797-802 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:64 year:1975 number:3 pages:797-802 http://dx.doi.org/10.1016/0006-291X(75)90117-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 64 1975 3 797-802 |
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(DE-627)NLEJ184200164 (DE-599)GBVNLZ184200164 DE-627 ger DE-627 rakwb eng Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Larry Cottam, G. oth Ward, R.L. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 64(1975), 3, Seite 797-802 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:64 year:1975 number:3 pages:797-802 http://dx.doi.org/10.1016/0006-291X(75)90117-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 64 1975 3 797-802 |
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fourier transform phosphorus magnetic resonance study of the interaction of p-enolpyruvate with the muscle pyruvate kinase-gadolinium complex |
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Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex |
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The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. |
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The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. |
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The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance. |
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