TY  - JOUR
AB  - Transglutaminase 1 (TGase1) is modified by myristoylation and palmitoylation supposedly in its cysteine cluster region. In order to monitor acylation in protein expression we developed a target mass spectrometry method using synthetic peptide SFWARCPalmCamGCamCamSCamR as a standard. It is palmitoylated at Cys6 and carbamidomethylated on the remaining cysteines to enable its use as surrogate peptide for the tryptically generated peptide from TGase1. The method allows the specific detection of the peptide based on its retention time in reversed-phase chromatography and its gas phase fragmentation pattern. In addition, the presence of a myristoyl group and of the peptide with no missed cleavages was programmed.
AU  - König, Simone
AU  - Bayer, Malte
AU  - Wiegmann, Henning
DA  - 2019-12
KW  - Transglutaminase 1
KW  - Ichthyose
KW  - Palmitoylierung
KW  - Myristoylierung
KW  - MRM
KW  - ichthyosis
KW  - palmitoylation
KW  - myristoylation
LA  - eng
IS  - Mercator Journal of Biomolecular Analysis
M2  - 1
PY  - 2019-12
SP  - 1-5
T2  - Mercator Journal of Biomolecular Analysis
TI  - Target analysis for the Cys-cluster tryptic peptide of acylated transglutaminase 1
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:6-12189607442
Y2  - 2024-12-26T20:20:21
ER  -