In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein
Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3...
Ausführliche Beschreibung
Autor*in: |
Small, D. H. [verfasserIn] Carnegie, P. R. [verfasserIn] |
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E-Artikel |
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Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1982 |
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Online-Ressource |
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Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 38(1982), 1, Seite 0 |
Übergeordnetes Werk: |
volume:38 ; year:1982 ; number:1 ; pages:0 |
Links: |
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DOI / URN: |
10.1111/j.1471-4159.1982.tb10870.x |
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10.1111/j.1471-4159.1982.tb10870.x doi (DE-627)NLEJ240318110 DE-627 ger DE-627 rakwb Small, D. H. verfasserin aut In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Carnegie, P. R. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb10870.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 1 0 |
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10.1111/j.1471-4159.1982.tb10870.x doi (DE-627)NLEJ240318110 DE-627 ger DE-627 rakwb Small, D. H. verfasserin aut In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Carnegie, P. R. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb10870.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 1 0 |
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10.1111/j.1471-4159.1982.tb10870.x doi (DE-627)NLEJ240318110 DE-627 ger DE-627 rakwb Small, D. H. verfasserin aut In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Carnegie, P. R. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb10870.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 1 0 |
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10.1111/j.1471-4159.1982.tb10870.x doi (DE-627)NLEJ240318110 DE-627 ger DE-627 rakwb Small, D. H. verfasserin aut In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Carnegie, P. R. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb10870.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 1 0 |
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10.1111/j.1471-4159.1982.tb10870.x doi (DE-627)NLEJ240318110 DE-627 ger DE-627 rakwb Small, D. H. verfasserin aut In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Carnegie, P. R. verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb10870.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 1 0 |
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Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. |
abstractGer |
Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. |
abstract_unstemmed |
Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days. |
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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">NLEJ240318110</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707110131.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1982 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1471-4159.1982.tb10870.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240318110</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">Small, D. H.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1982</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">Abstract: The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N′G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N′G-dimeth-ylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimeth-ylarginine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days.</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="650" ind1=" " ind2="4"><subfield code="a">Myelin basic protein</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Carnegie, P. R.</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 neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">38(1982), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:38</subfield><subfield code="g">year:1982</subfield><subfield code="g">number:1</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.1471-4159.1982.tb10870.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">38</subfield><subfield code="j">1982</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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