Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis
We developed an ultra-sensitive method of amino acid analysis (AAA) for the absolute quantification of less than 100 ng of proteins, in solution or on polyvinylidene difluoride (PVDF) membranes using an oxygen-free chamber for protein hydrolysis. We used a pre-label method with 6-aminoquinolyl- N -h...
Gespeichert in:
| Veröffentlicht in: | Analytical and bioanalytical chemistry 2013-10, Vol.405 (25), p.8073-8081 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 8081 |
|---|---|
| container_issue | 25 |
| container_start_page | 8073 |
| container_title | Analytical and bioanalytical chemistry |
| container_volume | 405 |
| creator | Masuda, Akiko Dohmae, Naoshi |
| description | We developed an ultra-sensitive method of amino acid analysis (AAA) for the absolute quantification of less than 100 ng of proteins, in solution or on polyvinylidene difluoride (PVDF) membranes using an oxygen-free chamber for protein hydrolysis. We used a pre-label method with 6-aminoquinolyl-
N
-hydroxysuccinimidyl carbamate for fluorescence detection, ion-pair chromatography with a reversed-phase column, and an ultra-high-pressure high-performance liquid chromatography. We optimized both handling- and instrument-dependent factors for accurate quantification and showed that the least amount of proteins to quantify was determined by handling accuracy rather than instrumental limit for quantification which was 0.6 fmol/amino acid. As a new evaluation method for the handling accuracy, we adopted the protein identification by the obtained amino acid compositions by AAA and the Swiss-Prot database search without the restriction of species. As a result, the least amount of starting material for AAA was 16 ng (0.24 pmol) for a solution of bovine serum albumin (BSA), 33 ng (0.50 pmol) for BSA on a PVDF membrane, and 44 ng (0.15 pmol) for thyroglobulin on a PVDF membrane. These results demonstrate that the ultra-sensitive AAA developed in this study is feasible for absolute quantification of biological significant protein.
Figure
Specification of ultra-sensitive amino acid analysis |
| doi_str_mv | 10.1007/s00216-013-7056-1 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3777156</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A352614258</galeid><sourcerecordid>A352614258</sourcerecordid><originalsourceid>FETCH-LOGICAL-c608t-2dbb73d295543d559ad0f507cbe49bea791b4ebfece9379bb258e65f8c778c1b3</originalsourceid><addsrcrecordid>eNqNkk9rFTEUxQdRbK1-ADcScNPN1PyZJJONUEqrQsGNrkOSuTMvZSZ5TWbE9-3NOPVRBVGySMj93XOTw6mq1wRfEIzlu4wxJaLGhNUSc1GTJ9UpEaStqeD46fHc0JPqRc53GBPeEvG8OqFMEqUYP62G6-9m8sHMPgYUe2QCMjbHcZkB3S8mzH4-rPcj5Izm3VpGuyV0CToUTIhDMlNegX2KM_iQkT2gVTEi43xX9Mx4yD6_rJ71Zszw6mE_q77eXH-5-ljffv7w6erytnYCt3NNO2sl66jivGEd58p0uOdYOguNsmCkIrYB24MDxaSylvIWBO9bJ2XriGVn1ftNd7_YCToHYU5m1PvkJ5MOOhqvf68Ev9ND_KaZlJJwUQTOHwRSvF8gz3ry2cE4mgBxyZoISRqGRcv_jTaSc0papv4DZY1suMIr-vYP9C4uqdj4czamjWolKdTFRg1mBO1DH8tvXFkdTN7FAL0v95eMU0GaYlJpIFuDSzHnBP3RE4L1mia9pUmXNOk1TXod8uaxmceOX_EpAN2AXEphgPTorX9V_QFITtWH</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1670249871</pqid></control><display><type>article</type><title>Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Masuda, Akiko ; Dohmae, Naoshi</creator><creatorcontrib>Masuda, Akiko ; Dohmae, Naoshi</creatorcontrib><description>We developed an ultra-sensitive method of amino acid analysis (AAA) for the absolute quantification of less than 100 ng of proteins, in solution or on polyvinylidene difluoride (PVDF) membranes using an oxygen-free chamber for protein hydrolysis. We used a pre-label method with 6-aminoquinolyl-
N
-hydroxysuccinimidyl carbamate for fluorescence detection, ion-pair chromatography with a reversed-phase column, and an ultra-high-pressure high-performance liquid chromatography. We optimized both handling- and instrument-dependent factors for accurate quantification and showed that the least amount of proteins to quantify was determined by handling accuracy rather than instrumental limit for quantification which was 0.6 fmol/amino acid. As a new evaluation method for the handling accuracy, we adopted the protein identification by the obtained amino acid compositions by AAA and the Swiss-Prot database search without the restriction of species. As a result, the least amount of starting material for AAA was 16 ng (0.24 pmol) for a solution of bovine serum albumin (BSA), 33 ng (0.50 pmol) for BSA on a PVDF membrane, and 44 ng (0.15 pmol) for thyroglobulin on a PVDF membrane. These results demonstrate that the ultra-sensitive AAA developed in this study is feasible for absolute quantification of biological significant protein.
Figure
Specification of ultra-sensitive amino acid analysis</description><identifier>ISSN: 1618-2642</identifier><identifier>EISSN: 1618-2650</identifier><identifier>DOI: 10.1007/s00216-013-7056-1</identifier><identifier>PMID: 23719935</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Accuracy ; Amino Acid Analysis ; Amino acids ; Amino Acids - analysis ; Aminoquinolines - chemistry ; Analytical Chemistry ; Animals ; Automation ; Biochemistry ; Carbamates - chemistry ; Cattle ; Characterization and Evaluation of Materials ; Chemical bonds ; Chemistry ; Chemistry and Materials Science ; Chromatography ; Chromatography, High Pressure Liquid - methods ; Chromatography, Reverse-Phase - methods ; Electrophoresis, Polyacrylamide Gel - methods ; Fluorescence ; Food Science ; Handling ; Hydrolysis ; Identification and classification ; Labeling ; Laboratory Medicine ; Limit of Detection ; Liquid chromatography ; Membrane proteins ; Membranes ; Membranes, Artificial ; Methods ; Monitoring/Environmental Analysis ; Nanostructure ; Peptides ; Polyvinylidene fluorides ; Polyvinyls - chemistry ; Proteins ; Proteins - analysis ; Proteolysis ; Proteomics ; Reagents ; Research Paper ; Searching ; Serum Albumin, Bovine - analysis ; Synthesis ; Thyroglobulin - analysis</subject><ispartof>Analytical and bioanalytical chemistry, 2013-10, Vol.405 (25), p.8073-8081</ispartof><rights>The Author(s) 2013</rights><rights>COPYRIGHT 2013 Springer</rights><rights>Springer-Verlag Berlin Heidelberg 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c608t-2dbb73d295543d559ad0f507cbe49bea791b4ebfece9379bb258e65f8c778c1b3</citedby><cites>FETCH-LOGICAL-c608t-2dbb73d295543d559ad0f507cbe49bea791b4ebfece9379bb258e65f8c778c1b3</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/s00216-013-7056-1$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00216-013-7056-1$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23719935$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Masuda, Akiko</creatorcontrib><creatorcontrib>Dohmae, Naoshi</creatorcontrib><title>Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis</title><title>Analytical and bioanalytical chemistry</title><addtitle>Anal Bioanal Chem</addtitle><addtitle>Anal Bioanal Chem</addtitle><description>We developed an ultra-sensitive method of amino acid analysis (AAA) for the absolute quantification of less than 100 ng of proteins, in solution or on polyvinylidene difluoride (PVDF) membranes using an oxygen-free chamber for protein hydrolysis. We used a pre-label method with 6-aminoquinolyl-
N
-hydroxysuccinimidyl carbamate for fluorescence detection, ion-pair chromatography with a reversed-phase column, and an ultra-high-pressure high-performance liquid chromatography. We optimized both handling- and instrument-dependent factors for accurate quantification and showed that the least amount of proteins to quantify was determined by handling accuracy rather than instrumental limit for quantification which was 0.6 fmol/amino acid. As a new evaluation method for the handling accuracy, we adopted the protein identification by the obtained amino acid compositions by AAA and the Swiss-Prot database search without the restriction of species. As a result, the least amount of starting material for AAA was 16 ng (0.24 pmol) for a solution of bovine serum albumin (BSA), 33 ng (0.50 pmol) for BSA on a PVDF membrane, and 44 ng (0.15 pmol) for thyroglobulin on a PVDF membrane. These results demonstrate that the ultra-sensitive AAA developed in this study is feasible for absolute quantification of biological significant protein.
Figure
Specification of ultra-sensitive amino acid analysis</description><subject>Accuracy</subject><subject>Amino Acid Analysis</subject><subject>Amino acids</subject><subject>Amino Acids - analysis</subject><subject>Aminoquinolines - chemistry</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Automation</subject><subject>Biochemistry</subject><subject>Carbamates - chemistry</subject><subject>Cattle</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemical bonds</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>Chromatography, Reverse-Phase - methods</subject><subject>Electrophoresis, Polyacrylamide Gel - methods</subject><subject>Fluorescence</subject><subject>Food Science</subject><subject>Handling</subject><subject>Hydrolysis</subject><subject>Identification and classification</subject><subject>Labeling</subject><subject>Laboratory Medicine</subject><subject>Limit of Detection</subject><subject>Liquid chromatography</subject><subject>Membrane proteins</subject><subject>Membranes</subject><subject>Membranes, Artificial</subject><subject>Methods</subject><subject>Monitoring/Environmental Analysis</subject><subject>Nanostructure</subject><subject>Peptides</subject><subject>Polyvinylidene fluorides</subject><subject>Polyvinyls - chemistry</subject><subject>Proteins</subject><subject>Proteins - analysis</subject><subject>Proteolysis</subject><subject>Proteomics</subject><subject>Reagents</subject><subject>Research Paper</subject><subject>Searching</subject><subject>Serum Albumin, Bovine - analysis</subject><subject>Synthesis</subject><subject>Thyroglobulin - analysis</subject><issn>1618-2642</issn><issn>1618-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNqNkk9rFTEUxQdRbK1-ADcScNPN1PyZJJONUEqrQsGNrkOSuTMvZSZ5TWbE9-3NOPVRBVGySMj93XOTw6mq1wRfEIzlu4wxJaLGhNUSc1GTJ9UpEaStqeD46fHc0JPqRc53GBPeEvG8OqFMEqUYP62G6-9m8sHMPgYUe2QCMjbHcZkB3S8mzH4-rPcj5Izm3VpGuyV0CToUTIhDMlNegX2KM_iQkT2gVTEi43xX9Mx4yD6_rJ71Zszw6mE_q77eXH-5-ljffv7w6erytnYCt3NNO2sl66jivGEd58p0uOdYOguNsmCkIrYB24MDxaSylvIWBO9bJ2XriGVn1ftNd7_YCToHYU5m1PvkJ5MOOhqvf68Ev9ND_KaZlJJwUQTOHwRSvF8gz3ry2cE4mgBxyZoISRqGRcv_jTaSc0papv4DZY1suMIr-vYP9C4uqdj4czamjWolKdTFRg1mBO1DH8tvXFkdTN7FAL0v95eMU0GaYlJpIFuDSzHnBP3RE4L1mia9pUmXNOk1TXod8uaxmceOX_EpAN2AXEphgPTorX9V_QFITtWH</recordid><startdate>20131001</startdate><enddate>20131001</enddate><creator>Masuda, Akiko</creator><creator>Dohmae, Naoshi</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>C6C</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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H8D</scope><scope>H8G</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>7QH</scope><scope>7UA</scope><scope>5PM</scope></search><sort><creationdate>20131001</creationdate><title>Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis</title><author>Masuda, Akiko ; Dohmae, Naoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c608t-2dbb73d295543d559ad0f507cbe49bea791b4ebfece9379bb258e65f8c778c1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Accuracy</topic><topic>Amino Acid Analysis</topic><topic>Amino acids</topic><topic>Amino Acids - analysis</topic><topic>Aminoquinolines - chemistry</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Automation</topic><topic>Biochemistry</topic><topic>Carbamates - chemistry</topic><topic>Cattle</topic><topic>Characterization and Evaluation of Materials</topic><topic>Chemical bonds</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>Chromatography, Reverse-Phase - methods</topic><topic>Electrophoresis, Polyacrylamide Gel - methods</topic><topic>Fluorescence</topic><topic>Food Science</topic><topic>Handling</topic><topic>Hydrolysis</topic><topic>Identification and classification</topic><topic>Labeling</topic><topic>Laboratory Medicine</topic><topic>Limit of Detection</topic><topic>Liquid chromatography</topic><topic>Membrane proteins</topic><topic>Membranes</topic><topic>Membranes, Artificial</topic><topic>Methods</topic><topic>Monitoring/Environmental Analysis</topic><topic>Nanostructure</topic><topic>Peptides</topic><topic>Polyvinylidene fluorides</topic><topic>Polyvinyls - chemistry</topic><topic>Proteins</topic><topic>Proteins - analysis</topic><topic>Proteolysis</topic><topic>Proteomics</topic><topic>Reagents</topic><topic>Research Paper</topic><topic>Searching</topic><topic>Serum Albumin, Bovine - analysis</topic><topic>Synthesis</topic><topic>Thyroglobulin - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Masuda, Akiko</creatorcontrib><creatorcontrib>Dohmae, Naoshi</creatorcontrib><collection>Springer Nature OA/Free Journals</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>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>ANTE: Abstracts in New Technology & Engineering</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>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>Aqualine</collection><collection>Water Resources Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Analytical and bioanalytical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Masuda, Akiko</au><au>Dohmae, Naoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis</atitle><jtitle>Analytical and bioanalytical chemistry</jtitle><stitle>Anal Bioanal Chem</stitle><addtitle>Anal Bioanal Chem</addtitle><date>2013-10-01</date><risdate>2013</risdate><volume>405</volume><issue>25</issue><spage>8073</spage><epage>8081</epage><pages>8073-8081</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>We developed an ultra-sensitive method of amino acid analysis (AAA) for the absolute quantification of less than 100 ng of proteins, in solution or on polyvinylidene difluoride (PVDF) membranes using an oxygen-free chamber for protein hydrolysis. We used a pre-label method with 6-aminoquinolyl-
N
-hydroxysuccinimidyl carbamate for fluorescence detection, ion-pair chromatography with a reversed-phase column, and an ultra-high-pressure high-performance liquid chromatography. We optimized both handling- and instrument-dependent factors for accurate quantification and showed that the least amount of proteins to quantify was determined by handling accuracy rather than instrumental limit for quantification which was 0.6 fmol/amino acid. As a new evaluation method for the handling accuracy, we adopted the protein identification by the obtained amino acid compositions by AAA and the Swiss-Prot database search without the restriction of species. As a result, the least amount of starting material for AAA was 16 ng (0.24 pmol) for a solution of bovine serum albumin (BSA), 33 ng (0.50 pmol) for BSA on a PVDF membrane, and 44 ng (0.15 pmol) for thyroglobulin on a PVDF membrane. These results demonstrate that the ultra-sensitive AAA developed in this study is feasible for absolute quantification of biological significant protein.
Figure
Specification of ultra-sensitive amino acid analysis</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>23719935</pmid><doi>10.1007/s00216-013-7056-1</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1618-2642 |
| ispartof | Analytical and bioanalytical chemistry, 2013-10, Vol.405 (25), p.8073-8081 |
| issn | 1618-2642 1618-2650 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3777156 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Accuracy Amino Acid Analysis Amino acids Amino Acids - analysis Aminoquinolines - chemistry Analytical Chemistry Animals Automation Biochemistry Carbamates - chemistry Cattle Characterization and Evaluation of Materials Chemical bonds Chemistry Chemistry and Materials Science Chromatography Chromatography, High Pressure Liquid - methods Chromatography, Reverse-Phase - methods Electrophoresis, Polyacrylamide Gel - methods Fluorescence Food Science Handling Hydrolysis Identification and classification Labeling Laboratory Medicine Limit of Detection Liquid chromatography Membrane proteins Membranes Membranes, Artificial Methods Monitoring/Environmental Analysis Nanostructure Peptides Polyvinylidene fluorides Polyvinyls - chemistry Proteins Proteins - analysis Proteolysis Proteomics Reagents Research Paper Searching Serum Albumin, Bovine - analysis Synthesis Thyroglobulin - analysis |
| title | Examination of an absolute quantity of less than a hundred nanograms of proteins by amino acid analysis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T12%3A04%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Examination%20of%20an%20absolute%20quantity%20of%20less%20than%20a%20hundred%20nanograms%20of%20proteins%20by%20amino%20acid%20analysis&rft.jtitle=Analytical%20and%20bioanalytical%20chemistry&rft.au=Masuda,%20Akiko&rft.date=2013-10-01&rft.volume=405&rft.issue=25&rft.spage=8073&rft.epage=8081&rft.pages=8073-8081&rft.issn=1618-2642&rft.eissn=1618-2650&rft_id=info:doi/10.1007/s00216-013-7056-1&rft_dat=%3Cgale_pubme%3EA352614258%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1670249871&rft_id=info:pmid/23719935&rft_galeid=A352614258&rfr_iscdi=true |