Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli
We have developed a method for the purification of tubulin from a parasitic nematode using DEAE-Sephadex column chromatography and temperature-dependent assembly. The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar prope...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1983-01, Vol.7 (3), p.267-277 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Dawson, Peter J. Gutteridge, Winston E. Gull, Keith |
| description | We have developed a method for the purification of tubulin from a parasitic nematode using DEAE-Sephadex column chromatography and temperature-dependent assembly. The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar properties to mammalian tubulin on one and two dimensional polyacrylamide gels, although certain electrophoretic conditions revealed a slight difference in the α-tubulins from mammals and nematodes. This was confirmed by limited proteolytic peptide mapping. The β subunit of nematode tubulin appeared almost identical to that of mammals. Peptide maps of these tubulins were also compared with those of eukaryotic micro-organisms and these results interpreted in terms of the evolution of the tubulin polypeptides and the sensitivity of helminths to antimicrotubular agents. |
| doi_str_mv | 10.1016/0166-6851(83)90026-9 |
| format | Article |
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The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar properties to mammalian tubulin on one and two dimensional polyacrylamide gels, although certain electrophoretic conditions revealed a slight difference in the α-tubulins from mammals and nematodes. This was confirmed by limited proteolytic peptide mapping. The β subunit of nematode tubulin appeared almost identical to that of mammals. Peptide maps of these tubulins were also compared with those of eukaryotic micro-organisms and these results interpreted in terms of the evolution of the tubulin polypeptides and the sensitivity of helminths to antimicrotubular agents.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(83)90026-9</identifier><identifier>PMID: 6888427</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Ascardia galli ; Ascaridia - analysis ; Ascaridia galli ; Ascaridiasis - parasitology ; Brain Chemistry ; Chickens ; Electrophoresis, Polyacrylamide Gel ; Microtubules ; Microtubules - analysis ; Microtubules - ultrastructure ; Nematode ; Nematode Infections - parasitology ; Peptide mapping ; Peptides - analysis ; Proteins, Nematoda ; Sheep ; Tubulin ; Tubulin - analysis ; Tubulin - isolation & purification</subject><ispartof>Molecular and biochemical parasitology, 1983-01, Vol.7 (3), p.267-277</ispartof><rights>1983</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-89b10f1dabd9c02fcf28dbe326d68db7ffab0214906cdc73ea4c86b96bc2c9b3</citedby><cites>FETCH-LOGICAL-c412t-89b10f1dabd9c02fcf28dbe326d68db7ffab0214906cdc73ea4c86b96bc2c9b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0166-6851(83)90026-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6888427$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dawson, Peter J.</creatorcontrib><creatorcontrib>Gutteridge, Winston E.</creatorcontrib><creatorcontrib>Gull, Keith</creatorcontrib><title>Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>We have developed a method for the purification of tubulin from a parasitic nematode using DEAE-Sephadex column chromatography and temperature-dependent assembly. The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar properties to mammalian tubulin on one and two dimensional polyacrylamide gels, although certain electrophoretic conditions revealed a slight difference in the α-tubulins from mammals and nematodes. This was confirmed by limited proteolytic peptide mapping. The β subunit of nematode tubulin appeared almost identical to that of mammals. Peptide maps of these tubulins were also compared with those of eukaryotic micro-organisms and these results interpreted in terms of the evolution of the tubulin polypeptides and the sensitivity of helminths to antimicrotubular agents.</description><subject>Animals</subject><subject>Ascardia galli</subject><subject>Ascaridia - analysis</subject><subject>Ascaridia galli</subject><subject>Ascaridiasis - parasitology</subject><subject>Brain Chemistry</subject><subject>Chickens</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Microtubules</subject><subject>Microtubules - analysis</subject><subject>Microtubules - ultrastructure</subject><subject>Nematode</subject><subject>Nematode Infections - parasitology</subject><subject>Peptide mapping</subject><subject>Peptides - analysis</subject><subject>Proteins, Nematoda</subject><subject>Sheep</subject><subject>Tubulin</subject><subject>Tubulin - analysis</subject><subject>Tubulin - isolation & purification</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF1rFTEQhoMo9bT6DxRzJRVcTbLZbHIjlOIXFBSsF16FZJK0kd3NaZIV_PfmuIde6sUwQ-aZl_Ag9IySN5RQ8baV6IQc6LnsXylCmOjUA7SjcmSd4kw-RLt75DE6LeUnIWQYhThBJ0JKydm4Qz--rjmGCKbGtGCzOAy3JhuoPseyPaaA62rXKS445DTjeuvxvjEl1gh48bOpyfnX-KKAydFFg2_MNMUn6FEwU_FPj_0MXX94f335qbv68vHz5cVVB5yy2kllKQnUGesUEBYgMOms75lwog1jCMYSRrkiAhyMvTccpLBKWGCgbH-GXm6x-5zuVl-qnmMBP01m8WktWhLRs2FQ_wUpZ5yPijeQbyDkVEr2Qe9znE3-rSnRB_P6oFUftGrZ67_m9SH_-TF_tbN390dH1W3_YtsHk7S5aXr192-M0L6dt-qHRrzbCN90_Yo-6wLRL-BdzB6qdin--wt_AGP0nVQ</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>Dawson, Peter J.</creator><creator>Gutteridge, Winston E.</creator><creator>Gull, Keith</creator><general>Elsevier B.V</general><scope>FBQ</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>19830101</creationdate><title>Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli</title><author>Dawson, Peter J. ; Gutteridge, Winston E. ; Gull, Keith</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-89b10f1dabd9c02fcf28dbe326d68db7ffab0214906cdc73ea4c86b96bc2c9b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Ascardia galli</topic><topic>Ascaridia - analysis</topic><topic>Ascaridia galli</topic><topic>Ascaridiasis - parasitology</topic><topic>Brain Chemistry</topic><topic>Chickens</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Microtubules</topic><topic>Microtubules - analysis</topic><topic>Microtubules - ultrastructure</topic><topic>Nematode</topic><topic>Nematode Infections - parasitology</topic><topic>Peptide mapping</topic><topic>Peptides - analysis</topic><topic>Proteins, Nematoda</topic><topic>Sheep</topic><topic>Tubulin</topic><topic>Tubulin - analysis</topic><topic>Tubulin - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dawson, Peter J.</creatorcontrib><creatorcontrib>Gutteridge, Winston E.</creatorcontrib><creatorcontrib>Gull, Keith</creatorcontrib><collection>AGRIS</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>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dawson, Peter J.</au><au>Gutteridge, Winston E.</au><au>Gull, Keith</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>7</volume><issue>3</issue><spage>267</spage><epage>277</epage><pages>267-277</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><abstract>We have developed a method for the purification of tubulin from a parasitic nematode using DEAE-Sephadex column chromatography and temperature-dependent assembly. The resulting microtubules were morphologically similar to those obtained from mammalian brain. The nematode tubulin showed similar properties to mammalian tubulin on one and two dimensional polyacrylamide gels, although certain electrophoretic conditions revealed a slight difference in the α-tubulins from mammals and nematodes. This was confirmed by limited proteolytic peptide mapping. The β subunit of nematode tubulin appeared almost identical to that of mammals. Peptide maps of these tubulins were also compared with those of eukaryotic micro-organisms and these results interpreted in terms of the evolution of the tubulin polypeptides and the sensitivity of helminths to antimicrotubular agents.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>6888427</pmid><doi>10.1016/0166-6851(83)90026-9</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0166-6851 |
| ispartof | Molecular and biochemical parasitology, 1983-01, Vol.7 (3), p.267-277 |
| issn | 0166-6851 1872-9428 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Ascardia galli Ascaridia - analysis Ascaridia galli Ascaridiasis - parasitology Brain Chemistry Chickens Electrophoresis, Polyacrylamide Gel Microtubules Microtubules - analysis Microtubules - ultrastructure Nematode Nematode Infections - parasitology Peptide mapping Peptides - analysis Proteins, Nematoda Sheep Tubulin Tubulin - analysis Tubulin - isolation & purification |
| title | Purification and characterisation of tubulin from the parasitic nematode, Ascaridia galli |
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