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

The rat liver mitochondrial proteins.

Michael Fountoulakis1, Peter Berndt, Hanno Langen

  • 1Genomics Technologies, F. Hoffmann-La Roche Ltd., Pharmaceutical Research, Basel, Switzerland. michael.fountoulakis@roche.com

Electrophoresis
|February 13, 2002
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

Impairment of Multiple Mitochondrial Energy Metabolism Pathways in the Heart of Chagas Disease Cardiomyopathy Patients.

Frontiers in immunology·2021
Same author

The Protein Profile of the Human Immature T-cell Line CCRF-CEM.

Cancer genomics & proteomics·2019
Same author

Proteomic Analysis of Liver from Transgenic Mice Overexpressing Small Heterodimer Partner.

Cancer genomics & proteomics·2019
Same author

[Distribution of mitoses and<sup>3</sup>H-thymidine incorporation in proliferating eye discs ofEphestia kuehniella Zeller].

Wilhelm Roux's archives of developmental biology·2017
Same author

Association of eukaryotic translation initiation factor eIF2B with fully solubilized CXCR4.

Journal of leukocyte biology·2015
Same author

Multiple procedures and cumulative individual radiation exposure in interventional cardiology: A long-term retrospective study.

European radiology·2015

Subcellular fractionation enhanced the detection of low-abundance mitochondrial proteins in rat liver. This proteomic analysis identified 192 gene products, including novel proteins, using advanced electrophoresis and mass spectrometry.

Area of Science:

  • Biochemistry
  • Proteomics
  • Cell Biology

Background:

  • Detecting low-abundance proteins is challenging in complex biological samples.
  • Subcellular fractionation enriches specific protein populations, improving detection sensitivity.
  • Mitochondria are crucial organelles with diverse protein functions, many present at low levels.

Purpose of the Study:

  • To develop and apply a method for enriching and identifying low-abundance mitochondrial proteins from rat liver.
  • To characterize the proteome of a highly enriched mitochondrial fraction.
  • To identify novel gene products within the mitochondrial proteome.

Main Methods:

  • Rat liver was subjected to subcellular fractionation to isolate mitochondria.
  • Proteins were separated using two-dimensional (2-D) electrophoresis with immobilized pH gradient strips.

Related Experiment Videos

  • Protein identification was performed using matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS).

    • Main Results:

    • 192 distinct gene products were identified in the mitochondrial-enriched fraction.
    • Approximately 70% of the identified proteins were enzymes, exhibiting a wide range of catalytic activities.
    • Eight gene products were identified for the first time, with most frequently detected proteins appearing as multiple spots.

    Conclusions:

    • Subcellular fractionation is effective for enhancing the detection of low-abundance proteins, particularly mitochondrial enzymes.
    • The applied proteomic approach successfully identified a significant number of mitochondrial proteins, including novel ones.
    • This methodology provides a valuable tool for deep proteome profiling and the discovery of new proteins in specific cellular compartments.