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

Glycophorin in lipid bilayers.

C W Grant, H M McConnell

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1974
    PubMed
    Summary

    Researchers studied human erythrocyte glycophorin, a major glycoprotein. Reincorporating it into lipid vesicles revealed its clustering and membrane interaction, confirming its role in cell recognition.

    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

    Baseline hydrocarbon levels in New Zealand coastal and marine avifauna.

    Marine pollution bulletin·2015
    Same author

    Spin-labeled membranes.

    The Journal of general physiology·2009
    Same author

    Contrast inversion in the epifluorescence of cholesterol-phospholipid monolayers.

    Biophysical journal·2004
    Same author

    Structural implications of a Val-->Glu mutation in transmembrane peptides from the EGF receptor.

    Biophysical journal·2001
    Same author

    Condensed complexes and the calorimetry of cholesterol-phospholipid bilayers.

    Biophysical journal·2001
    Same author

    Kinetics of registry selection of chimeric peptides binding to MHC II.

    Biochemistry·2001

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Membrane Biophysics

    Background:

    • Glycophorin is the primary glycoprotein in human red blood cells (erythrocytes).
    • Understanding its membrane integration and behavior is crucial for cell function and recognition.

    Purpose of the Study:

    • To investigate the structural and dynamic properties of isolated glycophorin reconstituted into artificial lipid vesicles.
    • To confirm the conformation and membrane interaction of glycophorin within a lipid bilayer.

    Main Methods:

    • Isolation and purification of human erythrocyte glycophorin.
    • Reconstitution of glycophorin into artificial lipid vesicles.
    • Freeze-fracture electron microscopy to visualize membrane structure and protein distribution.

    Main Results:

    • Reconstituted glycophorin appeared as particles on vesicle fracture faces, with a tendency to cluster.
    • Glycophorin penetrated the hydrophobic core of the lipid bilayer.
    • The N-terminal carbohydrate-rich region remained exposed to the aqueous environment.

    Conclusions:

    • Reconstituted glycophorin adopts a conformation similar to that in intact erythrocytes.
    • Glycophorin's structure facilitates its role as a specific recognition site on the cell surface.
    • The lipid-protein complex preferentially resides in fluid membrane regions.

    Related Experiment Videos