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WFRF:(Woessmann Jakob)
 

Sökning: WFRF:(Woessmann Jakob) > Assessing the Role ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004142naa a2200397 4500
001oai:DiVA.org:kth-349635
003SwePub
008240703s2023 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3496352 URI
0247 a https://doi.org/10.1021/acs.analchem.3c025432 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Woessmann, Jakobu KTH,Science for Life Laboratory, SciLifeLab,Systembiologi,Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark4 aut0 (Swepub:kth)u1zy02q9
2451 0a Assessing the Role of Trypsin in Quantitative Plasma and Single-Cell Proteomics toward Clinical Application
264 1b American Chemical Society (ACS),c 2023
338 a print2 rdacarrier
500 a QC 20240703
520 a Mass spectrometry-based bottom-up proteomics is rapidly evolving and routinely applied in large-scale biomedical studies. Proteases are a central component of every bottom-up proteomics experiment, digesting proteins into peptides. Trypsin has been the most widely applied protease in proteomics due to its characteristics. With ever-larger cohort sizes and possible future clinical application of mass spectrometry-based proteomics, the technical impact of trypsin becomes increasingly relevant. To assess possible biases introduced by trypsin digestion, we evaluated the impact of eight commercially available trypsins in a variety of bottom-up proteomics experiments and across a range of protease concentrations and storage times. To investigate the universal impact of these technical attributes, we included bulk HeLa cell lysate, human plasma, and single HEK293 cells, which were analyzed over a range of selected reaction monitoring (SRM), data-independent acquisition (DIA), and data-dependent acquisition (DDA) instrument methods on three LC-MS instruments. The quantification methods employed encompassed both label-free approaches and absolute quantification utilizing spike-in heavy-labeled recombinant protein fragment standards. Based on this extensive data set, we report variations between commercial trypsins, their source, and their concentration. Furthermore, we provide suggestions on the handling of trypsin in large-scale studies.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Petrosius, Valdemarasu Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark4 aut
7001 a Üresin, Nilu The Finsen Laboratory, Rigshospitalet, Faculty of Health Sciences and Biotech Research and Innovation Centre (BRIC), University of Copenhagen, 2200 Copenhagen, Denmark4 aut
7001 a Kotol, Davidu KTH,Systembiologi,Science for Life Laboratory, SciLifeLab4 aut0 (Swepub:kth)u1yd1hdh
7001 a Aragon-Fernandez, Pedrou Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark4 aut
7001 a Hober, Andreas,d 1992-u KTH,Science for Life Laboratory, SciLifeLab,Systembiologi4 aut0 (Swepub:kth)u15bkxsl
7001 a Auf Dem Keller, Ulrichu Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark4 aut
7001 a Edfors, Fredriku KTH,Science for Life Laboratory, SciLifeLab,Systembiologi4 aut0 (Swepub:kth)u149ml0e
7001 a Schoof, Erwin M.u Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark4 aut
7102 a KTHb Science for Life Laboratory, SciLifeLab4 org
7730 t Analytical Chemistryd : American Chemical Society (ACS)g 95:36, s. 13649-13658q 95:36<13649-13658x 0003-2700x 1520-6882
8564 u https://doi.org/10.1021/acs.analchem.3c02543y Fulltext
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-349635
8564 8u https://doi.org/10.1021/acs.analchem.3c02543

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