Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1
Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration....
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1979 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 89(1979), 4, Seite 1300-1306 |
| Übergeordnetes Werk: |
volume:89 ; year:1979 ; number:4 ; pages:1300-1306 |
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| 520 | |a Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. | ||
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(DE-627)NLEJ183524462 (DE-599)GBVNLZ183524462 DE-627 ger DE-627 rakwb eng Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Minkov, I.B. oth Fitin, A.F. oth Vasilyeva, E.A. oth Vinogradov, A.D. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 89(1979), 4, Seite 1300-1306 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:89 year:1979 number:4 pages:1300-1306 http://dx.doi.org/10.1016/0006-291X(79)92150-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 89 1979 4 1300-1306 |
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(DE-627)NLEJ183524462 (DE-599)GBVNLZ183524462 DE-627 ger DE-627 rakwb eng Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Minkov, I.B. oth Fitin, A.F. oth Vasilyeva, E.A. oth Vinogradov, A.D. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 89(1979), 4, Seite 1300-1306 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:89 year:1979 number:4 pages:1300-1306 http://dx.doi.org/10.1016/0006-291X(79)92150-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 89 1979 4 1300-1306 |
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(DE-627)NLEJ183524462 (DE-599)GBVNLZ183524462 DE-627 ger DE-627 rakwb eng Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Minkov, I.B. oth Fitin, A.F. oth Vasilyeva, E.A. oth Vinogradov, A.D. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 89(1979), 4, Seite 1300-1306 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:89 year:1979 number:4 pages:1300-1306 http://dx.doi.org/10.1016/0006-291X(79)92150-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 89 1979 4 1300-1306 |
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(DE-627)NLEJ183524462 (DE-599)GBVNLZ183524462 DE-627 ger DE-627 rakwb eng Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Minkov, I.B. oth Fitin, A.F. oth Vasilyeva, E.A. oth Vinogradov, A.D. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 89(1979), 4, Seite 1300-1306 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:89 year:1979 number:4 pages:1300-1306 http://dx.doi.org/10.1016/0006-291X(79)92150-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 89 1979 4 1300-1306 |
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(DE-627)NLEJ183524462 (DE-599)GBVNLZ183524462 DE-627 ger DE-627 rakwb eng Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Minkov, I.B. oth Fitin, A.F. oth Vasilyeva, E.A. oth Vinogradov, A.D. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 89(1979), 4, Seite 1300-1306 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:89 year:1979 number:4 pages:1300-1306 http://dx.doi.org/10.1016/0006-291X(79)92150-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 89 1979 4 1300-1306 |
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Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1 |
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Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. |
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Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. |
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Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system. |
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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">NLEJ183524462</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706204129.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1979 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183524462</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183524462</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">Mg^2^+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F"1</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1979</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">Incubation of F"1 in the presence of Mg^2^+ results in a pronounced lag in its ATPase activity measured with the ATP-regenerating system. A decrease of the initial rate of ATPase induced by Mg^2^+ is also observed when free nucleotides were separated from the enzyme by Sephadex gel filtration. No inhibition is observed when F"1 treated to remove tightly bound nucleotides was preincubated in the presence of Mg^2^+. Mg^2^+-induced inhibition of ATPase activity of nucleotide-depleted F"1 can be restored by an addition of low concentrations of ADP. In all cases the inhibited ATPase can be activated by the ADP-removing system /phosphoenol pyruvate + pyruvate kinase/. It is concluded that i/ Mg^2^+-induced inhibition of the ATPase activity of F"1 is due to the formation of an inactive F"1. ADP complex; and ii/ unusual inhibition of oligomycin-sensitive ATPase by ADP /Fitin et al., Biochem. Biophys. Res. Communs. 1979, 86, 434/ is directed to F"1 component of the complete mitochondrial ATPase system.</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">Minkov, I.B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Fitin, A.F.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vasilyeva, E.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vinogradov, A.D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">89(1979), 4, Seite 1300-1306</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:89</subfield><subfield code="g">year:1979</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:1300-1306</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0006-291X(79)92150-8</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">89</subfield><subfield code="j">1979</subfield><subfield code="e">4</subfield><subfield code="h">1300-1306</subfield></datafield></record></collection>
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7.397687 |