Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles
A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
REDDY, L. MOHAN [verfasserIn] CARPENTER, CHARLES E. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1991 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of food science - Chicago, Ill. : Inst., 1990, 56(1991), 5, Seite 0 |
| Übergeordnetes Werk: |
volume:56 ; year:1991 ; number:5 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-2621.1991.tb04724.x |
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| 520 | |a A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). | ||
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10.1111/j.1365-2621.1991.tb04724.x doi (DE-627)NLEJ240442652 DE-627 ger DE-627 rakwb REDDY, L. MOHAN verfasserin aut Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| CARPENTER, CHARLES E. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 56(1991), 5, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:56 year:1991 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb04724.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 5 0 |
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10.1111/j.1365-2621.1991.tb04724.x doi (DE-627)NLEJ240442652 DE-627 ger DE-627 rakwb REDDY, L. MOHAN verfasserin aut Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| CARPENTER, CHARLES E. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 56(1991), 5, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:56 year:1991 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb04724.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 5 0 |
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10.1111/j.1365-2621.1991.tb04724.x doi (DE-627)NLEJ240442652 DE-627 ger DE-627 rakwb REDDY, L. MOHAN verfasserin aut Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| CARPENTER, CHARLES E. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 56(1991), 5, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:56 year:1991 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb04724.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 5 0 |
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10.1111/j.1365-2621.1991.tb04724.x doi (DE-627)NLEJ240442652 DE-627 ger DE-627 rakwb REDDY, L. MOHAN verfasserin aut Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| CARPENTER, CHARLES E. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 56(1991), 5, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:56 year:1991 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb04724.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 5 0 |
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10.1111/j.1365-2621.1991.tb04724.x doi (DE-627)NLEJ240442652 DE-627 ger DE-627 rakwb REDDY, L. MOHAN verfasserin aut Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| CARPENTER, CHARLES E. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 56(1991), 5, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:56 year:1991 number:5 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1991.tb04724.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 56 1991 5 0 |
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determination of metmyoglobin reductase activity in bovine skeletal muscles |
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Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles |
| abstract |
A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). |
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A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). |
| abstract_unstemmed |
A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01). |
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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">NLEJ240442652</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707112039.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1991 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-2621.1991.tb04724.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240442652</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">REDDY, L. MOHAN</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Determination of Metmyoglobin Reductase Activity in Bovine Skeletal Muscles</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1991</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">A novel technique was used to obtain an isolate of skeletal muscle containing MetMb reductase. The isolate was then used as the enzyme source in an assay procedure to measure specific MetMb reductase activity. Enzyme activity was highest at pH 6.4 as compared to 5.8 or 7.0 and at 30°C compared to 4°C. Significant differences in enzyme activity were found among beef muscles from the same animal. The order of muscles, when enzyme activity was expressed on the basis of muscle myoglobin content, was: tensor faciae latae > longissimus dorsi > gluteus medius > diaphragma medialis > semimembranosus = psoas major (p = 0.01).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">CARPENTER, CHARLES E.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of food science</subfield><subfield code="d">Chicago, Ill. : Inst., 1990</subfield><subfield code="g">56(1991), 5, Seite 0</subfield><subfield code="w">(DE-627)NLEJ243926316</subfield><subfield code="w">(DE-600)2006705-7</subfield><subfield code="x">1750-3841</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:56</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:5</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.1365-2621.1991.tb04724.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">56</subfield><subfield code="j">1991</subfield><subfield code="e">5</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.398814 |