Proteolysis in mixed organic-aqueous solvent systems

Applications for peptide mass mapping using mass spectrometry

William Russell, Z. Y. Park, D. H. Russell

Research output: Contribution to journalArticle

230 Citations (Scopus)

Abstract

The rate of protein digestion imposes significant limitations on high-throughput protein identification using mass spectrometry. In this report, we demonstrate that proteins are readily digested by trypsin in the presence of organic solvents such as methanol, acetone, 2-propanol, and acetonitrile. The rates of protein digestion in organic solvents, as indicated by the abundances of digest fragment ions in the mass spectrum, are increased relative to aqueous solution. In addition, amino acid coverage for the analyzed proteins increases in the presence of the organic solvents, and proteins that are resistant to proteolysis are readily digested. For example, a 68% amino acid sequence coverage was attained from a tryptic digest of myoglobin in

Original languageEnglish (US)
Pages (from-to)2682-2685
Number of pages4
JournalAnalytical Chemistry
Volume73
Issue number11
DOIs
StatePublished - Jun 1 2001
Externally publishedYes

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Proteolysis
Mass spectrometry
Peptides
Organic solvents
Proteins
Amino Acids
2-Propanol
Myoglobin
Acetone
Trypsin
Methanol
Throughput
Ions

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Proteolysis in mixed organic-aqueous solvent systems : Applications for peptide mass mapping using mass spectrometry. / Russell, William; Park, Z. Y.; Russell, D. H.

In: Analytical Chemistry, Vol. 73, No. 11, 01.06.2001, p. 2682-2685.

Research output: Contribution to journalArticle

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