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

M. Setou; T. Hayasaka; S. Shimma; Y. Sugiura; M. Matsumoto

doi:10.1016/j.apsusc.2008.05.120

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

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

Research output: Contribution to journal › Article › peer-review

9 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 language	English
Pages (from-to)	1555-1559
Number of pages	5
Journal	Applied Surface Science
Volume	255
Issue number	4
DOIs	https://doi.org/10.1016/j.apsusc.2008.05.120
Publication status	Published - 2008 Dec 15
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Chemistry(all)
Condensed Matter Physics
Physics and Astronomy(all)
Surfaces and Interfaces
Surfaces, Coatings and Films

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10.1016/j.apsusc.2008.05.120

Cite this

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title = "Protein denaturation improves enzymatic digestion efficiency for direct tissue analysis using mass spectrometry",

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.",

keywords = "Brain, Denaturation, Digestion, MALDI-QIT-TOF MS, MS/MS analysis, Peptide",

author = "M. Setou and T. Hayasaka and S. Shimma and Y. Sugiura and M. Matsumoto",

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doi = "10.1016/j.apsusc.2008.05.120",

language = "English",

volume = "255",

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T1 - Protein denaturation improves enzymatic digestion efficiency for direct tissue analysis using mass spectrometry

AU - Setou, M.

AU - Hayasaka, T.

AU - Shimma, S.

AU - Sugiura, Y.

AU - Matsumoto, M.

PY - 2008/12/15

Y1 - 2008/12/15

N2 - 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.

AB - 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.

KW - Brain

KW - Denaturation

KW - Digestion

KW - MALDI-QIT-TOF MS

KW - MS/MS analysis

KW - Peptide

UR - http://www.scopus.com/inward/record.url?scp=56449131611&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=56449131611&partnerID=8YFLogxK

U2 - 10.1016/j.apsusc.2008.05.120

DO - 10.1016/j.apsusc.2008.05.120

M3 - Article

AN - SCOPUS:56449131611

SN - 0169-4332

VL - 255

SP - 1555

EP - 1559

JO - Applied Surface Science

JF - Applied Surface Science

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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