A novel approach for on-slide alkaline phosphatase digestion of previously analyzed samples

Suzanne M. Ramirez, Robert J. Cotter

Research output: Contribution to conferencePaper

Abstract

A new method was studied for phosphatase digestion on previously analyzed samples in 5 minutes at room temperatures, with reduced ionization suppression from the phosphatase. This method was first applied to a peptide with the sequence of RLEpSR and a M+H + of 741.3, observed by MALDI-TOF. The IMAC was utilized to isolate phosphorylated peptides from a tryptic digest of BSA and β-casein, a known phosphorlytaed protein. Phosphorylated peptides and peptides containing a high degree of aspartic and glutamic acids are isolated using this new method.

Original languageEnglish (US)
Pages317-318
Number of pages2
StatePublished - Dec 1 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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    Ramirez, S. M., & Cotter, R. J. (2002). A novel approach for on-slide alkaline phosphatase digestion of previously analyzed samples. 317-318. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.