Combined Method of Immunoaffinity Membrane Within Tubes and MALDI-TOF MS for Capturing and Analyzing Amyloid Beta
Amyloid beta 1-40 peptide was specifically isolated and analyzed from human plasma spiked with amyloid beta using a combined method of biotinylated anti-amyloid beta antibody binding to membrane-immobilized avidin (immunoaffinity membrane) and matrix-assisted laser desorption /ionization time-of-fli...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2015-12, Vol.177 (7), p.1565-1571 |
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| creator | Shimazaki, Youji Takatsu, Yoko |
| description | Amyloid beta 1-40 peptide was specifically isolated and analyzed from human plasma spiked with amyloid beta using a combined method of biotinylated anti-amyloid beta antibody binding to membrane-immobilized avidin (immunoaffinity membrane) and matrix-assisted laser desorption /ionization time-of-flight mass spectrometry (MALDI-TOF MS). A solution of 10 μL containing 13.6 ng to 2.9 μg of amyloid beta peptide was examined in this method. After the isolated amyloid beta peptide from the spiked human plasma containing 2.9 μg of amyloid beta peptide was incubated in the presence of trifluoroacetic acid, fibrillization of the peptides was observed using a thioflavin T assay. Furthermore, an immunoaffinity membrane present on the inner wall of a tube (diameter 2 mm) captured the amyloid beta peptide from the spiked human plasma. Our results indicate that the combination of the immunoaffinity membrane procedure and MALDI-TOF MS can be used to capture and analyze the target antigens such as amyloid beta in micro-spaces. |
| doi_str_mv | 10.1007/s12010-015-1837-2 |
| format | Article |
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A solution of 10 μL containing 13.6 ng to 2.9 μg of amyloid beta peptide was examined in this method. After the isolated amyloid beta peptide from the spiked human plasma containing 2.9 μg of amyloid beta peptide was incubated in the presence of trifluoroacetic acid, fibrillization of the peptides was observed using a thioflavin T assay. Furthermore, an immunoaffinity membrane present on the inner wall of a tube (diameter 2 mm) captured the amyloid beta peptide from the spiked human plasma. Our results indicate that the combination of the immunoaffinity membrane procedure and MALDI-TOF MS can be used to capture and analyze the target antigens such as amyloid beta in micro-spaces.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-015-1837-2</identifier><identifier>PMID: 26384493</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>amyloid ; Amyloid beta-Peptides - analysis ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - immunology ; Amyloid beta-Peptides - isolation & purification ; antibodies ; Antibodies, Immobilized - chemistry ; Antibodies, Immobilized - immunology ; antigens ; avidin ; Avidin - chemistry ; Biochemistry ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Chromatography, Affinity - methods ; desorption ; Humans ; Immunology ; Ionization ; Mass spectrometry ; matrix-assisted laser desorption-ionization mass spectrometry ; Membranes ; Membranes, Artificial ; Peptide Fragments - analysis ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - isolation & purification ; Peptides ; Plasma ; Protein Multimerization ; Protein Structure, Secondary ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><ispartof>Applied biochemistry and biotechnology, 2015-12, Vol.177 (7), p.1565-1571</ispartof><rights>Springer Science+Business Media New York 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-d2244103fcb01af230547f038f8f19377d38ad5a5a0931ac579c8e66fac730593</citedby><cites>FETCH-LOGICAL-c602t-d2244103fcb01af230547f038f8f19377d38ad5a5a0931ac579c8e66fac730593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-015-1837-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-015-1837-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26384493$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shimazaki, Youji</creatorcontrib><creatorcontrib>Takatsu, Yoko</creatorcontrib><title>Combined Method of Immunoaffinity Membrane Within Tubes and MALDI-TOF MS for Capturing and Analyzing Amyloid Beta</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Amyloid beta 1-40 peptide was specifically isolated and analyzed from human plasma spiked with amyloid beta using a combined method of biotinylated anti-amyloid beta antibody binding to membrane-immobilized avidin (immunoaffinity membrane) and matrix-assisted laser desorption /ionization time-of-flight mass spectrometry (MALDI-TOF MS). A solution of 10 μL containing 13.6 ng to 2.9 μg of amyloid beta peptide was examined in this method. After the isolated amyloid beta peptide from the spiked human plasma containing 2.9 μg of amyloid beta peptide was incubated in the presence of trifluoroacetic acid, fibrillization of the peptides was observed using a thioflavin T assay. Furthermore, an immunoaffinity membrane present on the inner wall of a tube (diameter 2 mm) captured the amyloid beta peptide from the spiked human plasma. Our results indicate that the combination of the immunoaffinity membrane procedure and MALDI-TOF MS can be used to capture and analyze the target antigens such as amyloid beta in micro-spaces.</description><subject>amyloid</subject><subject>Amyloid beta-Peptides - analysis</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - immunology</subject><subject>Amyloid beta-Peptides - isolation & purification</subject><subject>antibodies</subject><subject>Antibodies, Immobilized - chemistry</subject><subject>Antibodies, Immobilized - immunology</subject><subject>antigens</subject><subject>avidin</subject><subject>Avidin - chemistry</subject><subject>Biochemistry</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography, Affinity - methods</subject><subject>desorption</subject><subject>Humans</subject><subject>Immunology</subject><subject>Ionization</subject><subject>Mass spectrometry</subject><subject>matrix-assisted laser desorption-ionization mass spectrometry</subject><subject>Membranes</subject><subject>Membranes, Artificial</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Peptides</subject><subject>Plasma</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkUFv1DAQhS0EokvhB3ABS1y4GMZ2HDvHZWlhpa166FYcLSexW1dJvLWTw_Lr6zQFIQ6I02g033ujmYfQWwqfKID8nCgDCgSoIFRxSdgztKJCVARYRZ-jFTDJCWOqOkGvUroDoEwJ-RKdsJKroqj4Ct1vQl_7wbb4wo63ocXB4W3fT0MwzvnBj8c86OtoBot_-PHWD3g_1TZhM2TJevd1S_aX5_jiCrsQ8cYcxin64eZxvB5Md_w5d-v-2AXf4i92NK_RC2e6ZN881VN0fX6233wnu8tv2816R5oS2EhaxoqCAndNDdQ4xkEU0gFXTjlacSlbrkwrjDBQcWoaIatG2bJ0ppGZrfgp-rj4HmK4n2wade9TY7sunxKmpKkUlFEJpfwPlAvOSlGojH74C70LU8yHPlJclYLTeTddqCaGlKJ1-hB9b-JRU9BzdHqJTufo9BydZlnz7sl5qnvb_lb8yioDbAHSYX6xjX-s_ofr-0XkTNDmJvqkr68yVAIAA14AfwB246nR</recordid><startdate>20151201</startdate><enddate>20151201</enddate><creator>Shimazaki, Youji</creator><creator>Takatsu, Yoko</creator><general>Springer US</general><general>Springer Nature 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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope><scope>7TK</scope></search><sort><creationdate>20151201</creationdate><title>Combined Method of Immunoaffinity Membrane Within Tubes and MALDI-TOF MS for Capturing and Analyzing Amyloid Beta</title><author>Shimazaki, Youji ; Takatsu, Yoko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-d2244103fcb01af230547f038f8f19377d38ad5a5a0931ac579c8e66fac730593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>amyloid</topic><topic>Amyloid beta-Peptides - analysis</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Amyloid beta-Peptides - immunology</topic><topic>Amyloid beta-Peptides - isolation & purification</topic><topic>antibodies</topic><topic>Antibodies, Immobilized - chemistry</topic><topic>Antibodies, Immobilized - immunology</topic><topic>antigens</topic><topic>avidin</topic><topic>Avidin - chemistry</topic><topic>Biochemistry</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography, Affinity - methods</topic><topic>desorption</topic><topic>Humans</topic><topic>Immunology</topic><topic>Ionization</topic><topic>Mass spectrometry</topic><topic>matrix-assisted laser desorption-ionization mass spectrometry</topic><topic>Membranes</topic><topic>Membranes, Artificial</topic><topic>Peptide Fragments - analysis</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Peptides</topic><topic>Plasma</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Secondary</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shimazaki, Youji</creatorcontrib><creatorcontrib>Takatsu, Yoko</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>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shimazaki, Youji</au><au>Takatsu, Yoko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Combined Method of Immunoaffinity Membrane Within Tubes and MALDI-TOF MS for Capturing and Analyzing Amyloid Beta</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2015-12-01</date><risdate>2015</risdate><volume>177</volume><issue>7</issue><spage>1565</spage><epage>1571</epage><pages>1565-1571</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>Amyloid beta 1-40 peptide was specifically isolated and analyzed from human plasma spiked with amyloid beta using a combined method of biotinylated anti-amyloid beta antibody binding to membrane-immobilized avidin (immunoaffinity membrane) and matrix-assisted laser desorption /ionization time-of-flight mass spectrometry (MALDI-TOF MS). A solution of 10 μL containing 13.6 ng to 2.9 μg of amyloid beta peptide was examined in this method. After the isolated amyloid beta peptide from the spiked human plasma containing 2.9 μg of amyloid beta peptide was incubated in the presence of trifluoroacetic acid, fibrillization of the peptides was observed using a thioflavin T assay. Furthermore, an immunoaffinity membrane present on the inner wall of a tube (diameter 2 mm) captured the amyloid beta peptide from the spiked human plasma. Our results indicate that the combination of the immunoaffinity membrane procedure and MALDI-TOF MS can be used to capture and analyze the target antigens such as amyloid beta in micro-spaces.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>26384493</pmid><doi>10.1007/s12010-015-1837-2</doi><tpages>7</tpages></addata></record> |
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| subjects | amyloid Amyloid beta-Peptides - analysis Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - immunology Amyloid beta-Peptides - isolation & purification antibodies Antibodies, Immobilized - chemistry Antibodies, Immobilized - immunology antigens avidin Avidin - chemistry Biochemistry Biotechnology Chemistry Chemistry and Materials Science Chromatography, Affinity - methods desorption Humans Immunology Ionization Mass spectrometry matrix-assisted laser desorption-ionization mass spectrometry Membranes Membranes, Artificial Peptide Fragments - analysis Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - isolation & purification Peptides Plasma Protein Multimerization Protein Structure, Secondary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods |
| title | Combined Method of Immunoaffinity Membrane Within Tubes and MALDI-TOF MS for Capturing and Analyzing Amyloid Beta |
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