CALMODULIN IN SKELETAL MUSCLE
The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridg...
Ausführliche Beschreibung
Autor*in: |
HARTSHORNE, DAVID J. [verfasserIn] |
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Format: |
E-Artikel |
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Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1983 |
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Online-Ressource |
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Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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Übergeordnetes Werk: |
In: Journal of food biochemistry - Oxford [u.a.] : Wiley-Blackwell, 1977, 7(1983), 4, Seite 0 |
Übergeordnetes Werk: |
volume:7 ; year:1983 ; number:4 ; pages:0 |
Links: |
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DOI / URN: |
10.1111/j.1745-4514.1983.tb00799.x |
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520 | |a The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. | ||
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10.1111/j.1745-4514.1983.tb00799.x doi (DE-627)NLEJ240577582 DE-627 ger DE-627 rakwb HARTSHORNE, DAVID J. verfasserin aut CALMODULIN IN SKELETAL MUSCLE Oxford, UK Blackwell Publishing Ltd 1983 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| In Journal of food biochemistry Oxford [u.a.] : Wiley-Blackwell, 1977 7(1983), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927037 (DE-600)2174913-9 1745-4514 nnns volume:7 year:1983 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1983 4 0 |
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10.1111/j.1745-4514.1983.tb00799.x doi (DE-627)NLEJ240577582 DE-627 ger DE-627 rakwb HARTSHORNE, DAVID J. verfasserin aut CALMODULIN IN SKELETAL MUSCLE Oxford, UK Blackwell Publishing Ltd 1983 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| In Journal of food biochemistry Oxford [u.a.] : Wiley-Blackwell, 1977 7(1983), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927037 (DE-600)2174913-9 1745-4514 nnns volume:7 year:1983 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1983 4 0 |
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10.1111/j.1745-4514.1983.tb00799.x doi (DE-627)NLEJ240577582 DE-627 ger DE-627 rakwb HARTSHORNE, DAVID J. verfasserin aut CALMODULIN IN SKELETAL MUSCLE Oxford, UK Blackwell Publishing Ltd 1983 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| In Journal of food biochemistry Oxford [u.a.] : Wiley-Blackwell, 1977 7(1983), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927037 (DE-600)2174913-9 1745-4514 nnns volume:7 year:1983 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1983 4 0 |
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10.1111/j.1745-4514.1983.tb00799.x doi (DE-627)NLEJ240577582 DE-627 ger DE-627 rakwb HARTSHORNE, DAVID J. verfasserin aut CALMODULIN IN SKELETAL MUSCLE Oxford, UK Blackwell Publishing Ltd 1983 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| In Journal of food biochemistry Oxford [u.a.] : Wiley-Blackwell, 1977 7(1983), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927037 (DE-600)2174913-9 1745-4514 nnns volume:7 year:1983 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1983 4 0 |
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10.1111/j.1745-4514.1983.tb00799.x doi (DE-627)NLEJ240577582 DE-627 ger DE-627 rakwb HARTSHORNE, DAVID J. verfasserin aut CALMODULIN IN SKELETAL MUSCLE Oxford, UK Blackwell Publishing Ltd 1983 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| In Journal of food biochemistry Oxford [u.a.] : Wiley-Blackwell, 1977 7(1983), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927037 (DE-600)2174913-9 1745-4514 nnns volume:7 year:1983 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1983 4 0 |
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abstract |
The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. |
abstractGer |
The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. |
abstract_unstemmed |
The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality. |
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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">NLEJ240577582</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707114017.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1983 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1745-4514.1983.tb00799.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240577582</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="100" ind1="1" ind2=" "><subfield code="a">HARTSHORNE, DAVID J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">CALMODULIN IN SKELETAL MUSCLE</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1983</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">The central role of Ca2+ in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+ is attributable to the Ca2+-bindingprotein, troponin C. This protein in the presence of Ca2+ elicits conformational changes which allow cross-bridge cycling and hence contraction. Another Ca2+-binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin-dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat quality.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2007</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2007||||||||||</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of food biochemistry</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">7(1983), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927037</subfield><subfield code="w">(DE-600)2174913-9</subfield><subfield code="x">1745-4514</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:7</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1745-4514.1983.tb00799.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</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">7</subfield><subfield code="j">1983</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
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