Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Liquid chromatography MALDI MS/MS for membrane proteome analysis.

Nan Zhang1, Nan Li, Liang Li

  • 1Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2G2.

Journal of Proteome Research
|September 14, 2004
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[Biodegradation of o-chlorophenol by photosynthetic bacteria under co-metabolism].

Ying yong sheng tai xue bao = The journal of applied ecology·2011
Same author

Regulation of β-amyloid level in the brain of rats with cerebrovascular hypoperfusion.

Neurobiology of aging·2011
Same author

Nuclear factor high-mobility group box1 mediating the activation of Toll-like receptor 4 signaling in hepatocytes in the early stage of nonalcoholic fatty liver disease in mice.

Hepatology (Baltimore, Md.)·2011
Same author

"Chemical blowing" of thin-walled bubbles: high-throughput fabrication of large-area, few-layered BN and C(x) -BN nanosheets.

Advanced materials (Deerfield Beach, Fla.)·2011
Same author

Gemcitabine Cytotoxicity: Interaction of Efflux and Deamination.

Journal of drug metabolism & toxicology·2011
Same author

Tanghinigenin from seeds of Cerbera manghas L. induces apoptosis in human promyelocytic leukemia HL-60 cells.

Environmental toxicology and pharmacology·2011

Analyzing membrane proteins, crucial for biological functions and drug discovery, is challenging due to their hydrophobic nature. A new surfactant-aided shotgun proteomics method using LC/MALDI MS offers improved proteome coverage for these difficult targets.

Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Membrane proteins are vital for biological functions and drug discovery.
  • Their hydrophobic nature presents significant analytical challenges.
  • Current proteomic methods struggle with comprehensive membrane protein analysis.

Purpose of the Study:

  • To develop and evaluate a surfactant-aided shotgun proteomics approach for enhanced membrane proteome analysis.
  • To assess the utility of liquid chromatography/matrix-assisted laser desorption ionization (LC/MALDI) tandem mass spectrometry (MS) for membrane proteins.
  • To compare the performance of LC/MALDI with traditional gel electrophoresis/MS and 2D LC/electrospray ionization MS methods.

Main Methods:

  • Membrane proteins were solubilized and digested using sodium dodecyl sulfate (SDS).

Related Experiment Videos

  • Auto-offline liquid chromatography/matrix-assisted laser desorption ionization (LC/MALDI) tandem MS was employed for analysis.
  • One-dimensional (1D) LC separation was coupled with MALDI, leveraging SDS tolerance and a heated droplet interface for high flow rates.

    • Main Results:

    • The LC/MALDI approach demonstrated high tolerance to SDS, enabling direct analysis without extensive cleanup.
    • The method facilitated the detection of low-abundance proteins due to the use of larger sample amounts in 1D LC/MALDI.
    • LC/MALDI provided more extensive proteome coverage compared to gel electrophoresis/MS and 2D LC/electrospray ionization MS.

    Conclusions:

    • Surfactant-aided shotgun proteomics with LC/MALDI MS is an effective strategy for membrane proteome analysis.
    • This method enhances proteome coverage and simplifies sample handling for hydrophobic proteins.
    • Combining LC/MALDI with other proteomic techniques offers the most comprehensive approach to membrane proteome analysis.