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

Apolipoprotein C-III/sphingomyelin recombinants: formation, isolation, and characterization.

T Y Ahmad, J R Guyton, J T Sparrow

    Biochemistry
    |July 29, 1986
    PubMed
    Summary

    Apolipoprotein C-III (apoC-III) interaction with egg yolk sphingomyelin (EYSM) alters its structure and vesicle morphology. This study reveals how apoC-III binding induces structural changes in EYSM, impacting particle size and shape.

    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

    Synthesis of saturated, unsaturated, spin-labeled, and fluorescent cholesteryl esters: Acylation of cholesterol using fatty acid anhydride and 4-pyrrolidinopyridine.

    Lipids·2016
    Same author

    Tandem mass spectrometric characterization of a specific cysteic acid residue in oxidized human apoprotein B-100.

    Journal of the American Society for Mass Spectrometry·2013
    Same author

    Serum apolipoprotein C-III is independently associated with chronic hepatitis C infection and advanced fibrosis.

    Hepatology international·2011
    Same author

    Permeation of human plasma lipoproteins in human carotid endarterectomy tissues: measurement by optical coherence tomography.

    Journal of lipid research·2011
    Same author

    Lipid-altering efficacy and safety profile of combination therapy with ezetimibe/statin vs. statin monotherapy in patients with and without diabetes: an analysis of pooled data from 27 clinical trials.

    Diabetes, obesity & metabolism·2011
    Same author

    Time dependent changes in aortic tissue during cold storage in physiological solution.

    Biochimica et biophysica acta·2011

    Area of Science:

    • Biochemistry
    • Lipid-protein interactions
    • Structural biology

    Background:

    • Apolipoprotein C-III (apoC-III) is a key lipoprotein component involved in lipid metabolism.
    • Sphingomyelin (SM) is a major phospholipid in cell membranes.
    • Understanding protein-lipid interactions is crucial for elucidating biological processes.

    Purpose of the Study:

    • To investigate the structural changes of apolipoprotein C-III (apoC-III) upon binding to egg yolk sphingomyelin (EYSM).
    • To characterize the morphological alterations of EYSM vesicles induced by apoC-III.
    • To determine the effect of protein:lipid ratio on complex formation and structure.

    Main Methods:

    • Circular dichroism spectroscopy to assess alpha-helical content.
    • Tryptophan fluorescence spectroscopy to monitor protein conformational changes.

    Related Experiment Videos

  • Gel filtration chromatography and sedimentation velocity to analyze complex size and stability.
  • Electron microscopy to visualize structural morphology.

    • Main Results:

    • ApoC-III's alpha-helical content increased from 20% to 67% with increasing EYSM concentration.
    • Tryptophan fluorescence showed a blue shift, indicating a more hydrophobic environment for apoC-III.
    • EYSM vesicles disintegrated into smaller particles, forming disk-shaped structures with increasing apoC-III.
    • Disk diameter reduced to 204 ± 34 Å, while thickness remained constant at 51 ± 2 Å.

    Conclusions:

    • Apolipoprotein C-III binding induces significant conformational changes in its alpha-helical structure.
    • ApoC-III binding leads to the disruption of sphingomyelin vesicles and formation of smaller, disk-like structures.
    • The study provides insights into the molecular mechanisms of apoC-III-lipid interactions and their structural consequences.