Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain
Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide pa...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Berlet, Hans H. [verfasserIn] Ilzenhöfer, Heike [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1985 |
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| Schlagwörter: |
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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 neurochemistry - Oxford : Wiley-Blackwell, 1956, 45(1985), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:45 ; year:1985 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1471-4159.1985.tb05482.x |
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| 520 | |a Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. | ||
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10.1111/j.1471-4159.1985.tb05482.x doi (DE-627)NLEJ240298705 DE-627 ger DE-627 rakwb Berlet, Hans H. verfasserin aut Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Oxford, UK Blackwell Publishing Ltd 1985 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Ilzenhöfer, Heike verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 45(1985), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:45 year:1985 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1985 1 0 |
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10.1111/j.1471-4159.1985.tb05482.x doi (DE-627)NLEJ240298705 DE-627 ger DE-627 rakwb Berlet, Hans H. verfasserin aut Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Oxford, UK Blackwell Publishing Ltd 1985 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Ilzenhöfer, Heike verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 45(1985), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:45 year:1985 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1985 1 0 |
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10.1111/j.1471-4159.1985.tb05482.x doi (DE-627)NLEJ240298705 DE-627 ger DE-627 rakwb Berlet, Hans H. verfasserin aut Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Oxford, UK Blackwell Publishing Ltd 1985 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Ilzenhöfer, Heike verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 45(1985), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:45 year:1985 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1985 1 0 |
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10.1111/j.1471-4159.1985.tb05482.x doi (DE-627)NLEJ240298705 DE-627 ger DE-627 rakwb Berlet, Hans H. verfasserin aut Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Oxford, UK Blackwell Publishing Ltd 1985 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Ilzenhöfer, Heike verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 45(1985), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:45 year:1985 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1985 1 0 |
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10.1111/j.1471-4159.1985.tb05482.x doi (DE-627)NLEJ240298705 DE-627 ger DE-627 rakwb Berlet, Hans H. verfasserin aut Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Oxford, UK Blackwell Publishing Ltd 1985 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Myelin basic protein Ilzenhöfer, Heike verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 45(1985), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:45 year:1985 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 1985 1 0 |
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Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. |
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Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. |
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Abstract: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP. |
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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">NLEJ240298705</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707105826.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1985 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1471-4159.1985.tb05482.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240298705</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">Berlet, Hans H.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1985</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: Acid extracts of delipidated white matter of bovine brain were prepared, and their proteolytic activities toward myelin basic protein (MBP) were evaluated at pH 3 and pH 7. This was done by measuring changes in total protein using a selective dye-binding assay, and by evaluating peptide patterns by sodium dodecyl sulfate-poly-acrylamide gel electrophoresis and densitometry. At pH 7 >50% of total protein and about 75% of MBP were degraded after 48 h, whereas at pH 3 it was <20% altogether. Neutral proteolysis of MBP entailed up to 12 different proteolytic peptide fragments in the molecular weight range of 17.5 to 6 kd. Its enzymatic nature was verified using protease inhibitors, including N-ethylmale-imide, phenylmethylsulfonyl fluoride, o-phenanthroline, and EDTA, as well as pepstatin A and α2macroglobulin. Both transient changes in percentages of some intermediate peptides and differential effects of individual inhibitors on electrophoretic peptide patterns strongly suggest a sequential type of limited proteolysis. The results also indicate that acid extracts contained several endopepti-dases of which a cysteine protease appears to initiate the breakdown of MBP.</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">Ilzenhöfer, Heike</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">45(1985), 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:45</subfield><subfield code="g">year:1985</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.1471-4159.1985.tb05482.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">45</subfield><subfield code="j">1985</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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