The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity
Tubulin carboxypeptidase was found to be inhibited by myelin basic protein in a concentration dependent manner. The inhibition was produced by the interaction between myelin basic protein with the substrate. As a consequence of this interaction, turbid insoluble aggregates were formed at either 5° o...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1986-04, Vol.136 (2), p.482-489 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 489 |
|---|---|
| container_issue | 2 |
| container_start_page | 482 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 136 |
| creator | Modesti, Nidia M. Barra, Héctor S. |
| description | Tubulin carboxypeptidase was found to be inhibited by myelin basic protein in a concentration dependent manner. The inhibition was produced by the interaction between myelin basic protein with the substrate. As a consequence of this interaction, turbid insoluble aggregates were formed at either 5° or 37°C. The turbidity increased by increasing the myelin basic protein concentration and it reached a plateau at a molar ratio of myelin basic protein to tubulin dimer of about 6. At plateau, the molar ratio in the insoluble aggregates was about 6. When tubulin was in excess, the formation of the insoluble aggregates was diminished. However, if the excess of tubulin was added after the formation of the aggregates, the turbidity was not significantly affected. Turbidity was diminished by increasing the ionic strength. |
| doi_str_mv | 10.1016/0006-291X(86)90466-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76838853</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X86904663</els_id><sourcerecordid>76838853</sourcerecordid><originalsourceid>FETCH-LOGICAL-c417t-36abb21b9e49f4b2c51b6c747457a4fa9858fa6ffb3846915bf926780e19a2903</originalsourceid><addsrcrecordid>eNqFkUtLJDEUhYM4aPv4Bwq1kEEXNeZVqWQjiKgzIMxGwV1IUjd0pLqqTVJq__upstteOqsQzncO956L0AnBvwgm4hJjLEqqyPO5FBcKcyFKtoNmBCtcUoL5LpptkX10kNILxoRwofbQHuWUYclmqH2cQxG6DNG4HPqu6H2xWEEbusKaFFyxjH2G8fce8rzIgx0myXRNkT-N82DDl-9LdSba_mO1hGUOjUlQTNFvIa-O0A9v2gTHm_cQPd3dPt78Lh_-3v-5uX4oHSd1Lpkw1lJiFXDluaWuIla4mte8qg33RslKeiO8t0yO65DKekVFLTEQZajC7BD9XOeOw78OkLJehOSgbU0H_ZB0LSSTsmL_Bce2aiJYPYJ8DbrYpxTB62UMCxNXmmA9XUNPVeupai2F_ryGnvJPN_mDXUCzNW3qH_WzjW6SM62PpnMhbTFJsKRSjNjVGoOxtLcAUScXoHPQhAgu66YP38_xDyfop3s</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14671637</pqid></control><display><type>article</type><title>The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Modesti, Nidia M. ; Barra, Héctor S.</creator><creatorcontrib>Modesti, Nidia M. ; Barra, Héctor S.</creatorcontrib><description>Tubulin carboxypeptidase was found to be inhibited by myelin basic protein in a concentration dependent manner. The inhibition was produced by the interaction between myelin basic protein with the substrate. As a consequence of this interaction, turbid insoluble aggregates were formed at either 5° or 37°C. The turbidity increased by increasing the myelin basic protein concentration and it reached a plateau at a molar ratio of myelin basic protein to tubulin dimer of about 6. At plateau, the molar ratio in the insoluble aggregates was about 6. When tubulin was in excess, the formation of the insoluble aggregates was diminished. However, if the excess of tubulin was added after the formation of the aggregates, the turbidity was not significantly affected. Turbidity was diminished by increasing the ionic strength.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(86)90466-3</identifier><identifier>PMID: 2423083</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Applied sciences ; Brain - enzymology ; Carboxypeptidases - antagonists & inhibitors ; Cattle ; Exact sciences and technology ; Immunologic Techniques ; Kinetics ; Macromolecular Substances ; myelin basic protein ; Myelin Basic Protein - metabolism ; Myelin Basic Protein - pharmacology ; Nephelometry and Turbidimetry ; Osmolar Concentration ; Other techniques and industries ; Tubulin - metabolism ; tubulin carboxypeptidase</subject><ispartof>Biochemical and biophysical research communications, 1986-04, Vol.136 (2), p.482-489</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-36abb21b9e49f4b2c51b6c747457a4fa9858fa6ffb3846915bf926780e19a2903</citedby><cites>FETCH-LOGICAL-c417t-36abb21b9e49f4b2c51b6c747457a4fa9858fa6ffb3846915bf926780e19a2903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(86)90466-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8108286$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2423083$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Modesti, Nidia M.</creatorcontrib><creatorcontrib>Barra, Héctor S.</creatorcontrib><title>The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Tubulin carboxypeptidase was found to be inhibited by myelin basic protein in a concentration dependent manner. The inhibition was produced by the interaction between myelin basic protein with the substrate. As a consequence of this interaction, turbid insoluble aggregates were formed at either 5° or 37°C. The turbidity increased by increasing the myelin basic protein concentration and it reached a plateau at a molar ratio of myelin basic protein to tubulin dimer of about 6. At plateau, the molar ratio in the insoluble aggregates was about 6. When tubulin was in excess, the formation of the insoluble aggregates was diminished. However, if the excess of tubulin was added after the formation of the aggregates, the turbidity was not significantly affected. Turbidity was diminished by increasing the ionic strength.</description><subject>Animals</subject><subject>Applied sciences</subject><subject>Brain - enzymology</subject><subject>Carboxypeptidases - antagonists & inhibitors</subject><subject>Cattle</subject><subject>Exact sciences and technology</subject><subject>Immunologic Techniques</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>myelin basic protein</subject><subject>Myelin Basic Protein - metabolism</subject><subject>Myelin Basic Protein - pharmacology</subject><subject>Nephelometry and Turbidimetry</subject><subject>Osmolar Concentration</subject><subject>Other techniques and industries</subject><subject>Tubulin - metabolism</subject><subject>tubulin carboxypeptidase</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLJDEUhYM4aPv4Bwq1kEEXNeZVqWQjiKgzIMxGwV1IUjd0pLqqTVJq__upstteOqsQzncO956L0AnBvwgm4hJjLEqqyPO5FBcKcyFKtoNmBCtcUoL5LpptkX10kNILxoRwofbQHuWUYclmqH2cQxG6DNG4HPqu6H2xWEEbusKaFFyxjH2G8fce8rzIgx0myXRNkT-N82DDl-9LdSba_mO1hGUOjUlQTNFvIa-O0A9v2gTHm_cQPd3dPt78Lh_-3v-5uX4oHSd1Lpkw1lJiFXDluaWuIla4mte8qg33RslKeiO8t0yO65DKekVFLTEQZajC7BD9XOeOw78OkLJehOSgbU0H_ZB0LSSTsmL_Bce2aiJYPYJ8DbrYpxTB62UMCxNXmmA9XUNPVeupai2F_ryGnvJPN_mDXUCzNW3qH_WzjW6SM62PpnMhbTFJsKRSjNjVGoOxtLcAUScXoHPQhAgu66YP38_xDyfop3s</recordid><startdate>19860429</startdate><enddate>19860429</enddate><creator>Modesti, Nidia M.</creator><creator>Barra, Héctor S.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19860429</creationdate><title>The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity</title><author>Modesti, Nidia M. ; Barra, Héctor S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-36abb21b9e49f4b2c51b6c747457a4fa9858fa6ffb3846915bf926780e19a2903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>Applied sciences</topic><topic>Brain - enzymology</topic><topic>Carboxypeptidases - antagonists & inhibitors</topic><topic>Cattle</topic><topic>Exact sciences and technology</topic><topic>Immunologic Techniques</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>myelin basic protein</topic><topic>Myelin Basic Protein - metabolism</topic><topic>Myelin Basic Protein - pharmacology</topic><topic>Nephelometry and Turbidimetry</topic><topic>Osmolar Concentration</topic><topic>Other techniques and industries</topic><topic>Tubulin - metabolism</topic><topic>tubulin carboxypeptidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Modesti, Nidia M.</creatorcontrib><creatorcontrib>Barra, Héctor S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Modesti, Nidia M.</au><au>Barra, Héctor S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1986-04-29</date><risdate>1986</risdate><volume>136</volume><issue>2</issue><spage>482</spage><epage>489</epage><pages>482-489</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Tubulin carboxypeptidase was found to be inhibited by myelin basic protein in a concentration dependent manner. The inhibition was produced by the interaction between myelin basic protein with the substrate. As a consequence of this interaction, turbid insoluble aggregates were formed at either 5° or 37°C. The turbidity increased by increasing the myelin basic protein concentration and it reached a plateau at a molar ratio of myelin basic protein to tubulin dimer of about 6. At plateau, the molar ratio in the insoluble aggregates was about 6. When tubulin was in excess, the formation of the insoluble aggregates was diminished. However, if the excess of tubulin was added after the formation of the aggregates, the turbidity was not significantly affected. Turbidity was diminished by increasing the ionic strength.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2423083</pmid><doi>10.1016/0006-291X(86)90466-3</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1986-04, Vol.136 (2), p.482-489 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76838853 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Applied sciences Brain - enzymology Carboxypeptidases - antagonists & inhibitors Cattle Exact sciences and technology Immunologic Techniques Kinetics Macromolecular Substances myelin basic protein Myelin Basic Protein - metabolism Myelin Basic Protein - pharmacology Nephelometry and Turbidimetry Osmolar Concentration Other techniques and industries Tubulin - metabolism tubulin carboxypeptidase |
| title | The interaction of myelin basic protein with tubulin and the inhibition of tubulin carboxypeptidase activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T03%3A40%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20interaction%20of%20myelin%20basic%20protein%20with%20tubulin%20and%20the%20inhibition%20of%20tubulin%20carboxypeptidase%20activity&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Modesti,%20Nidia%20M.&rft.date=1986-04-29&rft.volume=136&rft.issue=2&rft.spage=482&rft.epage=489&rft.pages=482-489&rft.issn=0006-291X&rft.eissn=1090-2104&rft.coden=BBRCA9&rft_id=info:doi/10.1016/0006-291X(86)90466-3&rft_dat=%3Cproquest_cross%3E76838853%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14671637&rft_id=info:pmid/2423083&rft_els_id=0006291X86904663&rfr_iscdi=true |