ISSN: 0974-276X
Linda Nagore
University of Texas at San Antonio, USA
Posters-Accepted Abstracts: J Proteomics Bioinform
The common difficulty with any enrichment technique is developing a method that can be widely applicable and yet still extract a small subset of the proteome. We discuss a high-throughput MALDI-MS method that uses DNA to enrich for transcriptions factors while simultaneously removing interfering sample components. This was accomplished by using a polyvinylpyrrolidone coated MALDI plate which has the unique advantage of enrichment, desalting, digestion and characterization on a single platform. Protein as well as DNA can be analyzed directly from the support. This approach positively identified five transcription factors from nuclear extract using the hTERT promoter using MS/MS of a discrete set of tryptic peptides. On-target enrichment coupled to MALDI-TOF-MS has shown to be fast, sensitive and highly reproducible with low redundancy and can be applied to any protein that binds DNA including those with low affinities.
Email: linda.nagore@gmail.com