Protein denaturation improves enzymatic digestion efficiency for direct tissue analysis using mass spectrometry

M. Setou, T. Hayasaka, S. Shimma, Yuki Sugiura, M. Matsumoto

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Molecular identification using high-sensitivity tandem mass spectrometry is essential for protein analysis on the tissue surface. Here we report an improved digestion protocol for protein identification directly on the tissue surface using mass spectrometry. By denaturation process and the use of detergent-supplemented trypsin solution, we could successfully detect and identify many molecules such as tubulin, neurofilament, and synaptosomal-associated 25 kDa protein directly from a mouse cerebellum section.

Original languageEnglish
Pages (from-to)1555-1559
Number of pages5
JournalApplied Surface Science
Volume255
Issue number4
DOIs
Publication statusPublished - 2008 Dec 15
Externally publishedYes

Fingerprint

Denaturation
Mass spectrometry
Tissue
Proteins
Detergents
Tubulin
Trypsin
Molecules

Keywords

  • Brain
  • Denaturation
  • Digestion
  • MALDI-QIT-TOF MS
  • MS/MS analysis
  • Peptide

ASJC Scopus subject areas

  • Surfaces, Coatings and Films

Cite this

Protein denaturation improves enzymatic digestion efficiency for direct tissue analysis using mass spectrometry. / Setou, M.; Hayasaka, T.; Shimma, S.; Sugiura, Yuki; Matsumoto, M.

In: Applied Surface Science, Vol. 255, No. 4, 15.12.2008, p. 1555-1559.

Research output: Contribution to journalArticle

Setou, M. ; Hayasaka, T. ; Shimma, S. ; Sugiura, Yuki ; Matsumoto, M. / Protein denaturation improves enzymatic digestion efficiency for direct tissue analysis using mass spectrometry. In: Applied Surface Science. 2008 ; Vol. 255, No. 4. pp. 1555-1559.
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