There are dozens of post-tranlational modifications out there, but there aren't enough techniques to study them all. Lysine acetylation has been studied before, but few labs work on this modification as opposed to phosphorylation due to lack of optimized protocols. A new paper from Steve Carr's lab on characterization of lysine acetylome using an optimized protocol is an effort in this direction. The authors combined 7 monoclonal antibodies with specificity for lysine acetylated peptides and used this for enrichment. They used this method with Jurkat cells and combined it with a SILAC approach for quantitation. The authors identified over 10,000 lysine acetylated peptides from over 3,000 proteins!!
They applied this method to breast cancer xenografts and used TMT and iTRAQ for quantitation. Over 6,700 acetylated peptides from over 2,300 proteins were identified.
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