Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline
Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane N...
Ausführliche Beschreibung
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| Autor*in: |
Chkadua, Gvantsa [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 |
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| Übergeordnetes Werk: |
Enthalten in: Cell biochemistry and biophysics - New York, NY : Springer, 1979, 80(2021), 1 vom: 26. Aug., Seite 23-29 |
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| Übergeordnetes Werk: |
volume:80 ; year:2021 ; number:1 ; day:26 ; month:08 ; pages:23-29 |
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| DOI / URN: |
10.1007/s12013-021-01032-6 |
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SPR046346422 |
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| 520 | |a Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. | ||
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10.1007/s12013-021-01032-6 doi (DE-627)SPR046346422 (SPR)s12013-021-01032-6-e DE-627 ger DE-627 rakwb eng Chkadua, Gvantsa verfasserin (orcid)0000-0001-6492-8818 aut Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 Nozadze, Eka aut Tsakadze, Leila aut Shioshvili, Lia aut Leladze, Marine aut Arutinova, Nana aut Dzneladze, Sopio aut Javakhishvili, Maia aut Kupradze, Sopio aut Enthalten in Cell biochemistry and biophysics New York, NY : Springer, 1979 80(2021), 1 vom: 26. Aug., Seite 23-29 (DE-627)342893793 (DE-600)2072590-5 1559-0283 nnns volume:80 year:2021 number:1 day:26 month:08 pages:23-29 https://dx.doi.org/10.1007/s12013-021-01032-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 80 2021 1 26 08 23-29 |
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10.1007/s12013-021-01032-6 doi (DE-627)SPR046346422 (SPR)s12013-021-01032-6-e DE-627 ger DE-627 rakwb eng Chkadua, Gvantsa verfasserin (orcid)0000-0001-6492-8818 aut Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 Nozadze, Eka aut Tsakadze, Leila aut Shioshvili, Lia aut Leladze, Marine aut Arutinova, Nana aut Dzneladze, Sopio aut Javakhishvili, Maia aut Kupradze, Sopio aut Enthalten in Cell biochemistry and biophysics New York, NY : Springer, 1979 80(2021), 1 vom: 26. Aug., Seite 23-29 (DE-627)342893793 (DE-600)2072590-5 1559-0283 nnns volume:80 year:2021 number:1 day:26 month:08 pages:23-29 https://dx.doi.org/10.1007/s12013-021-01032-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 80 2021 1 26 08 23-29 |
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10.1007/s12013-021-01032-6 doi (DE-627)SPR046346422 (SPR)s12013-021-01032-6-e DE-627 ger DE-627 rakwb eng Chkadua, Gvantsa verfasserin (orcid)0000-0001-6492-8818 aut Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 Nozadze, Eka aut Tsakadze, Leila aut Shioshvili, Lia aut Leladze, Marine aut Arutinova, Nana aut Dzneladze, Sopio aut Javakhishvili, Maia aut Kupradze, Sopio aut Enthalten in Cell biochemistry and biophysics New York, NY : Springer, 1979 80(2021), 1 vom: 26. Aug., Seite 23-29 (DE-627)342893793 (DE-600)2072590-5 1559-0283 nnns volume:80 year:2021 number:1 day:26 month:08 pages:23-29 https://dx.doi.org/10.1007/s12013-021-01032-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 80 2021 1 26 08 23-29 |
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10.1007/s12013-021-01032-6 doi (DE-627)SPR046346422 (SPR)s12013-021-01032-6-e DE-627 ger DE-627 rakwb eng Chkadua, Gvantsa verfasserin (orcid)0000-0001-6492-8818 aut Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 Nozadze, Eka aut Tsakadze, Leila aut Shioshvili, Lia aut Leladze, Marine aut Arutinova, Nana aut Dzneladze, Sopio aut Javakhishvili, Maia aut Kupradze, Sopio aut Enthalten in Cell biochemistry and biophysics New York, NY : Springer, 1979 80(2021), 1 vom: 26. Aug., Seite 23-29 (DE-627)342893793 (DE-600)2072590-5 1559-0283 nnns volume:80 year:2021 number:1 day:26 month:08 pages:23-29 https://dx.doi.org/10.1007/s12013-021-01032-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 80 2021 1 26 08 23-29 |
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10.1007/s12013-021-01032-6 doi (DE-627)SPR046346422 (SPR)s12013-021-01032-6-e DE-627 ger DE-627 rakwb eng Chkadua, Gvantsa verfasserin (orcid)0000-0001-6492-8818 aut Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 Nozadze, Eka aut Tsakadze, Leila aut Shioshvili, Lia aut Leladze, Marine aut Arutinova, Nana aut Dzneladze, Sopio aut Javakhishvili, Maia aut Kupradze, Sopio aut Enthalten in Cell biochemistry and biophysics New York, NY : Springer, 1979 80(2021), 1 vom: 26. Aug., Seite 23-29 (DE-627)342893793 (DE-600)2072590-5 1559-0283 nnns volume:80 year:2021 number:1 day:26 month:08 pages:23-29 https://dx.doi.org/10.1007/s12013-021-01032-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 80 2021 1 26 08 23-29 |
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Enthalten in Cell biochemistry and biophysics 80(2021), 1 vom: 26. Aug., Seite 23-29 volume:80 year:2021 number:1 day:26 month:08 pages:23-29 |
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Chkadua, Gvantsa @@aut@@ Nozadze, Eka @@aut@@ Tsakadze, Leila @@aut@@ Shioshvili, Lia @@aut@@ Leladze, Marine @@aut@@ Arutinova, Nana @@aut@@ Dzneladze, Sopio @@aut@@ Javakhishvili, Maia @@aut@@ Kupradze, Sopio @@aut@@ |
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Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. 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Chkadua, Gvantsa |
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Chkadua, Gvantsa misc Na,K-ATPase misc Neurotransmitter misc Enzyme kinetics misc Multi-sited enzyme systems Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline |
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Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline Na,K-ATPase (dpeaa)DE-He213 Neurotransmitter (dpeaa)DE-He213 Enzyme kinetics (dpeaa)DE-He213 Multi-sited enzyme systems (dpeaa)DE-He213 |
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Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline |
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Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline |
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Chkadua, Gvantsa |
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Cell biochemistry and biophysics |
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Chkadua, Gvantsa Nozadze, Eka Tsakadze, Leila Shioshvili, Lia Leladze, Marine Arutinova, Nana Dzneladze, Sopio Javakhishvili, Maia Kupradze, Sopio |
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Chkadua, Gvantsa |
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some kinetic features of na,k-atpase and sensitivity to noradrenaline |
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Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline |
| abstract |
Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 |
| abstractGer |
Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 |
| abstract_unstemmed |
Abstract A comparative kinetic analysis of albino rat brain synaptic and kidney plasma membrane fraction Na,K-ATPase was performed to comprehend the different levels of sensitivity of these fractions to the neurotransmitter noradrenaline. Noradrenaline (NA) inhibits the rat brain synaptic membrane Na,K-ATPase, changes the stoichiometry of $ Na^{+} $ and $ K^{+} $ and shifts the enzyme system from an MgATP to an $ Mg^{2+} $ dependent cycle. While the kidney plasma membrane fraction Na,K-ATPase is not sensitive to noradrenaline. To investigate the mechanism underlying this difference, we studied enzyme velocity dependence on the concentration of $ Mg^{2+} $. The 1/V = f($ Mg^{2+} $) function has shown different kinetic features for the synaptic and kidney plasma membrane Na,K-ATPase. With the addition of ethylene glycol tetraacetic acid (EGTA) to the reaction medium the geometric form of 1/V = f($ Mg^{2+} $) function is affected differently. We thereafter measured the essential activator number for $ Na^{+} $ and $ K^{+} $ with, in excess $ Mg^{2+} $. The results of these experiments reveal that, contrary to the synaptic membrane Na,K-ATPase, the kidney plasma membrane fraction Na,K-ATPase does not possess an $ Mg^{2+} $ dependent cycle and noradrenaline exhibits different modulatory effects on the enzyme system. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 |
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| title_short |
Some Kinetic Features of Na,K-ATPase and Sensitivity to Noradrenaline |
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https://dx.doi.org/10.1007/s12013-021-01032-6 |
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| author2 |
Nozadze, Eka Tsakadze, Leila Shioshvili, Lia Leladze, Marine Arutinova, Nana Dzneladze, Sopio Javakhishvili, Maia Kupradze, Sopio |
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Nozadze, Eka Tsakadze, Leila Shioshvili, Lia Leladze, Marine Arutinova, Nana Dzneladze, Sopio Javakhishvili, Maia Kupradze, Sopio |
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10.1007/s12013-021-01032-6 |
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| score |
7.398961 |