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Evaluation of 2,6-dihydroxyacetophenone as matrix-assisted laser desorption/ionization matrix for analysis of hydrophobic proteins and peptides
KTH, School of Chemical Science and Engineering (CHE), Chemistry.ORCID iD: 0000-0003-3548-217X
KTH, School of Chemical Science and Engineering (CHE), Chemistry.ORCID iD: 0000-0002-3444-9987
2012 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 425, no 1, 18-20 p.Article in journal (Refereed) Published
Abstract [en]

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is widely used for analysis of macromolecules like peptides and proteins. The analysis procedure is generally simple but must be adapted to the characteristics of the analytes. Therefore, specific matrices suitable for, e.g., hydrophobic proteins and peptides that are difficult to analyze would be preferable in order to optimize the outcome. In the present work, 2,6-dihydroxyacetophenone (DHAP) was shown to be beneficial in comparison to DHB for intact bacteriorhodopsin (BR) as well as for chemically digested BR.

Place, publisher, year, edition, pages
2012. Vol. 425, no 1, 18-20 p.
Keyword [en]
DHAP, Hydrophobic protein/peptides, MALDI-MS, Matrix
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-96183DOI: 10.1016/j.ab.2012.02.039ISI: 000303950100004ScopusID: 2-s2.0-84859323545OAI: diva2:529926
Swedish Research Council, 621-2009-4095
QC 20120531Available from: 2012-05-31 Created: 2012-05-31 Last updated: 2012-06-07Bibliographically approved

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