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
Autor*in: |
Berlet, Hans H. [verfasserIn] Ilzenhöfer, Heike [verfasserIn] |
---|
Format: |
E-Artikel |
---|
Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1985 |
---|
Schlagwörter: |
---|
Umfang: |
Online-Ressource |
---|
Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
---|---|
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 |
Links: |
---|
DOI / URN: |
10.1111/j.1471-4159.1985.tb05482.x |
---|
Katalog-ID: |
NLEJ240298705 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | NLEJ240298705 | ||
003 | DE-627 | ||
005 | 20210707105826.0 | ||
007 | cr uuu---uuuuu | ||
008 | 120426s1985 xx |||||o 00| ||und c | ||
024 | 7 | |a 10.1111/j.1471-4159.1985.tb05482.x |2 doi | |
035 | |a (DE-627)NLEJ240298705 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
100 | 1 | |a Berlet, Hans H. |e verfasserin |4 aut | |
245 | 1 | 0 | |a Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
264 | 1 | |a Oxford, UK |b Blackwell Publishing Ltd |c 1985 | |
300 | |a Online-Ressource | ||
336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
337 | |a nicht spezifiziert |b z |2 rdamedia | ||
338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
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. | ||
533 | |d 2006 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2006|||||||||| | ||
650 | 4 | |a Myelin basic protein | |
700 | 1 | |a Ilzenhöfer, Heike |e verfasserin |4 aut | |
773 | 0 | 8 | |i In |t Journal of neurochemistry |d Oxford : Wiley-Blackwell, 1956 |g 45(1985), 1, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243927584 |w (DE-600)2020528-4 |x 1471-4159 |7 nnns |
773 | 1 | 8 | |g volume:45 |g year:1985 |g number:1 |g pages:0 |
856 | 4 | 0 | |u http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
912 | |a GBV_USEFLAG_U | ||
912 | |a ZDB-1-DJB | ||
912 | |a GBV_NL_ARTICLE | ||
951 | |a AR | ||
952 | |d 45 |j 1985 |e 1 |h 0 |
author_variant |
h h b hh hhb h i hi |
---|---|
matchkey_str |
article:14714159:1985----::euniliiepoelssfylnaipoenyetapoesa |
hierarchy_sort_str |
1985 |
publishDate |
1985 |
allfields |
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 |
spelling |
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 |
allfields_unstemmed |
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 |
allfieldsGer |
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 |
allfieldsSound |
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 |
source |
In Journal of neurochemistry 45(1985), 1, Seite 0 volume:45 year:1985 number:1 pages:0 |
sourceStr |
In Journal of neurochemistry 45(1985), 1, Seite 0 volume:45 year:1985 number:1 pages:0 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
topic_facet |
Myelin basic protein |
isfreeaccess_bool |
false |
container_title |
Journal of neurochemistry |
authorswithroles_txt_mv |
Berlet, Hans H. @@aut@@ Ilzenhöfer, Heike @@aut@@ |
publishDateDaySort_date |
1985-01-01T00:00:00Z |
hierarchy_top_id |
NLEJ243927584 |
id |
NLEJ240298705 |
fullrecord |
<?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>
|
series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
author |
Berlet, Hans H. |
spellingShingle |
Berlet, Hans H. misc Myelin basic protein Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
authorStr |
Berlet, Hans H. |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243927584 |
format |
electronic Article |
delete_txt_mv |
keep |
author_role |
aut aut |
collection |
NL |
publishPlace |
Oxford, UK |
remote_str |
true |
illustrated |
Not Illustrated |
issn |
1471-4159 |
topic_title |
Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain Myelin basic protein |
publisher |
Blackwell Publishing Ltd |
publisherStr |
Blackwell Publishing Ltd |
topic |
misc Myelin basic protein |
topic_unstemmed |
misc Myelin basic protein |
topic_browse |
misc Myelin basic protein |
format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
zu |
hierarchy_parent_title |
Journal of neurochemistry |
hierarchy_parent_id |
NLEJ243927584 |
hierarchy_top_title |
Journal of neurochemistry |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)NLEJ243927584 (DE-600)2020528-4 |
title |
Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
ctrlnum |
(DE-627)NLEJ240298705 |
title_full |
Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
author_sort |
Berlet, Hans H. |
journal |
Journal of neurochemistry |
journalStr |
Journal of neurochemistry |
isOA_bool |
false |
recordtype |
marc |
publishDateSort |
1985 |
contenttype_str_mv |
zzz |
container_start_page |
0 |
author_browse |
Berlet, Hans H. Ilzenhöfer, Heike |
container_volume |
45 |
physical |
Online-Ressource |
format_se |
Elektronische Aufsätze |
author-letter |
Berlet, Hans H. |
doi_str_mv |
10.1111/j.1471-4159.1985.tb05482.x |
author2-role |
verfasserin |
title_sort |
sequential limited proteolysis of myelin basic protein by neutral protease activities of bovine brain |
title_auth |
Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
abstract |
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. |
abstractGer |
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. |
abstract_unstemmed |
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. |
collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
container_issue |
1 |
title_short |
Sequential Limited Proteolysis of Myelin Basic Protein by Neutral Protease Activities of Bovine Brain |
url |
http://dx.doi.org/10.1111/j.1471-4159.1985.tb05482.x |
remote_bool |
true |
author2 |
Ilzenhöfer, Heike |
author2Str |
Ilzenhöfer, Heike |
ppnlink |
NLEJ243927584 |
mediatype_str_mv |
z |
isOA_txt |
false |
hochschulschrift_bool |
false |
doi_str |
10.1111/j.1471-4159.1985.tb05482.x |
up_date |
2024-07-06T09:37:56.196Z |
_version_ |
1803821961650896896 |
fullrecord_marcxml |
<?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>
|
score |
7.4019423 |