^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase
^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with...
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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: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 169(1975), 1, Seite 22-28 |
| Übergeordnetes Werk: |
volume:169 ; year:1975 ; number:1 ; pages:22-28 |
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| 245 | 1 | 0 | |a ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase |
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| 520 | |a ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. | ||
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(DE-627)NLEJ183380487 (DE-599)GBVNLZ183380487 DE-627 ger DE-627 rakwb eng ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 169(1975), 1, Seite 22-28 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:169 year:1975 number:1 pages:22-28 http://dx.doi.org/10.1016/0003-9861(75)90312-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 169 1975 1 22-28 |
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(DE-627)NLEJ183380487 (DE-599)GBVNLZ183380487 DE-627 ger DE-627 rakwb eng ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 169(1975), 1, Seite 22-28 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:169 year:1975 number:1 pages:22-28 http://dx.doi.org/10.1016/0003-9861(75)90312-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 169 1975 1 22-28 |
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(DE-627)NLEJ183380487 (DE-599)GBVNLZ183380487 DE-627 ger DE-627 rakwb eng ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 169(1975), 1, Seite 22-28 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:169 year:1975 number:1 pages:22-28 http://dx.doi.org/10.1016/0003-9861(75)90312-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 169 1975 1 22-28 |
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(DE-627)NLEJ183380487 (DE-599)GBVNLZ183380487 DE-627 ger DE-627 rakwb eng ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 169(1975), 1, Seite 22-28 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:169 year:1975 number:1 pages:22-28 http://dx.doi.org/10.1016/0003-9861(75)90312-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 169 1975 1 22-28 |
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(DE-627)NLEJ183380487 (DE-599)GBVNLZ183380487 DE-627 ger DE-627 rakwb eng ^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier ^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 169(1975), 1, Seite 22-28 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:169 year:1975 number:1 pages:22-28 http://dx.doi.org/10.1016/0003-9861(75)90312-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 169 1975 1 22-28 |
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^3^5cl nuclear magnetic resonance studies of anion-binding sites in proteins: lactate dehydrogenase |
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^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase |
| abstract |
^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. |
| abstractGer |
^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. |
| abstract_unstemmed |
^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ183380487</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706201718.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1975 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183380487</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183380487</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">^3^5Cl nuclear magnetic resonance studies of anion-binding sites in proteins: Lactate dehydrogenase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1975</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">^3^5Cl nmr relaxation rate measurements have been used to study anion-binding sites in pig heart lactate dehydrogenase. These studies reveal two types of sites, one is intimately associated with the active site, the other is not. The nonactive site has been ascribed to a subunit site in analogy with crystallographic results from the dogfish M"4 enzyme. The binding of either the reduced or the oxidized form of NAD results in an increase in the ^3^5Cl nmr relaxation rate by a factor of 1.8-2. The enhanced nmr relaxation rate of the binary lactate dehydrogenase-NAD complex is reduced on binding of the substrate inhibitor molecules oxamate or oxalate to a value less than that exhibited by lactate dehydrogenase alone. The enhancement of the nmr relaxation rate is attributed to a decrease in the dissociation constant of Cl for the enzyme. The K"p values for Cl binding to the active center site of lactate dehydrogenase is 0.85 m and for lactate dehydrogenase-NADH is 0.25 m. The ratio of these constants, 3.4, agrees well with the measured enhancement value 3.7. The effect of coenzyme analogs on the ^3^5Cl nmr relaxation rate has been examined. 3-Acetylpyridine NAD produces an enhancement of 4.3, thionicotinamide NAD of 2.3, whereas 3-pyridinealdehyde, adenosinediphosphoribose, and adenosine diphosphate do not affect the nmr relaxation state of Cl bound to lactate dehydrogenase.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ward, R.L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Archives of Biochemistry and Biophysics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">169(1975), 1, Seite 22-28</subfield><subfield code="w">(DE-627)NLEJ177020539</subfield><subfield code="w">(DE-600)1461378-5</subfield><subfield code="x">0003-9861</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:169</subfield><subfield code="g">year:1975</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:22-28</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(75)90312-4</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">169</subfield><subfield code="j">1975</subfield><subfield code="e">1</subfield><subfield code="h">22-28</subfield></datafield></record></collection>
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