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Proteinase K improves quantitative acylation studies

Title data

Fränzel, Benjamin ; Fischer, Frank ; Steegborn, Clemens ; Wolters, Dirk:
Proteinase K improves quantitative acylation studies.
In: Proteomics. Vol. 15 (January 2015) Issue 1 . - pp. 44-47.
ISSN 1615-9861
DOI: https://doi.org/10.1002/pmic.201400015

Abstract in another language

Acetylation is a common PTM of proteins but is still challenging to analyze. Only few acetylome studies have been performed to tackle this issue. Yet, the detection of acetylated proteins in complex cell lysates remains to be improved. Here, we present a proteomic approach with proteinase K as a suitable protease to identify acetylated peptides quantitatively. We first optimized the digestion conditions using an artificial system of purified bovine histones to find the optimal protease. Subsequently, the capability of proteinase K was demonstrated in complex HEK293 cell lysates. Finally, SILAC in combination with MudPIT was used to show that quantification with proteinase K is possible. In this study, we identified a sheer number of 557 unique acetylated peptides originating from 633 acetylation sites.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 25332194
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 20 Apr 2015 14:28
Last Modified: 03 Jul 2015 09:01
URI: https://eref.uni-bayreuth.de/id/eprint/10433