Abstract
Protein N-terminal acetylation is a widespread modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs). The various NATs and their specific substrate specificities and catalytic mechanisms are far from fully understood. We here describe an in vitro method based on reverse-phase HPLC to quantitatively measure in vitro acetylation of NAT oligopeptide substrates, enabling the determination of NAT specificity as well as kinetic parameters.
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References
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Acknowledgements
P.V.D. is a postdoctoral fellow of the research foundation—Flanders (FWO-Vlaanderen). K.G. acknowledges support of research grants from the Fund for Scientific Research—Flanders (Belgium) (project numbers G.0042.07 and G.0440.10), the Concerted Research Actions (project BOF07/GOA/012) from the Ghent University, and the Inter University Attraction Poles (IUAP06). T.A. is supported by the Norwegian Research Council (Grant 197136), and the Norwegian Cancer Society.
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Evjenth, R.H., Van Damme, P., Gevaert, K., Arnesen, T. (2013). HPLC-Based Quantification of In Vitro N-Terminal Acetylation. In: Hake, S., Janzen, C. (eds) Protein Acetylation. Methods in Molecular Biology, vol 981. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-305-3_7
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DOI: https://doi.org/10.1007/978-1-62703-305-3_7
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Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-304-6
Online ISBN: 978-1-62703-305-3
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