Automated integration of monolith-based protein separation with on-plate digestion for mass spectrometric analysis of esophageal adenocarcinoma human epithelial samples
dc.contributor.author | Yoo, Chul | en_US |
dc.contributor.author | Zhao, Jia | en_US |
dc.contributor.author | Pal, Manoj | en_US |
dc.contributor.author | Hersberger, Katherine | en_US |
dc.contributor.author | Huber, Christian G. | en_US |
dc.contributor.author | Simeone, Diane M. | en_US |
dc.contributor.author | Beer, David G. | en_US |
dc.contributor.author | Lubman, David M. | en_US |
dc.date.accessioned | 2007-09-18T19:24:16Z | |
dc.date.available | 2007-09-18T19:24:16Z | |
dc.date.issued | 2006-09 | en_US |
dc.identifier.citation | Yoo, Chul; Zhao, Jia; Pal, Manoj; Hersberger, Katherine; Huber, Christian G.; Simeone, Diane M.; Beer, David G.; Lubman, David M. (2006). "Automated integration of monolith-based protein separation with on-plate digestion for mass spectrometric analysis of esophageal adenocarcinoma human epithelial samples." Electrophoresis 27(18): 3643-3651. <http://hdl.handle.net/2027.42/55811> | en_US |
dc.identifier.issn | 0173-0835 | en_US |
dc.identifier.issn | 1522-2683 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/55811 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=16927349&dopt=citation | en_US |
dc.description.abstract | A unique approach of automating the integration of monolithic capillary HPLC-based protein separation and on-plate digestion for subsequent MALDI-MS analysis has been developed. All liquid-handling procedures were performed using a robotic module. This automated high-throughput method minimizes the amount of time and extensive labor required for traditional in-solution digestion followed by exhaustive sample cleanup and analysis. Also, precise positioning of the droplet from the capillary HPLC separation onto the MALDI plate allows for preconcentration effects of analytes for improved sensitivity. Proteins from primary esophageal Barrett's adenocarcinoma tissue were prefractionated by chromatofocusing and analyzed successfully by this automated configuration, obtaining rapid protein identifications through PMF and sequencing analyses with high sequence coverage. Additionally, intact protein molecular weight values were obtained as a means to further confirm protein identification and also to identify potential sequence modifications of proteins. This simple and rapid method is a highly versatile and robust approach for the analysis of complex proteomes. | en_US |
dc.format.extent | 309199 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Biochemistry and Biotechnology | en_US |
dc.title | Automated integration of monolith-based protein separation with on-plate digestion for mass spectrometric analysis of esophageal adenocarcinoma human epithelial samples | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Surgery, The University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Surgery, The University of Michigan Medical Center, Ann Arbor, MI, USA ; Comprehensive Cancer Center, University of Michigan Medical Center, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI, USA ; Department of Surgery, The University of Michigan Medical Center, Ann Arbor, MI, USA ; Comprehensive Cancer Center, University of Michigan Medical Center, Ann Arbor, MI, USA ; The University of Michigan Medical Center, 1150 West Medical Center Dr, MSRB1 RMA510B, Ann Arbor, MI 48109, USA Fax: +1-734-763-6199 | en_US |
dc.contributor.affiliationother | Department of Chemistry, Instrumental Analysis and Bioanalysis, Saarland University, SaarbrÜcken, Germany | en_US |
dc.identifier.pmid | 16927349 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/55811/1/3643_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/elps.200600117 | en_US |
dc.identifier.source | Electrophoresis | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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