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

Human erythrocyte myosin: identification and purification.

V M Fowler, J Q Davis, V Bennett

    The Journal of Cell Biology
    |January 1, 1985
    PubMed
    Summary

    Human red blood cells contain myosin, a protein crucial for cell shape and movement. This study identifies and characterizes erythrocyte myosin, revealing its potential role in cellular structure and function.

    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

    KLF1 coordinates specialized transcriptional networks required to maintain the integrity of terminal erythropoiesis.

    Journal of cell science·2025
    Same author

    Management of iatrogenic bronchial tear during one-lung ventilation for robotic thoracic surgery.

    Anaesthesia reports·2025
    Same author

    Lipopolysaccharide structure modulates cationic biocide susceptibility and crystalline biofilm formation in <i>Proteus mirabilis</i>.

    Frontiers in microbiology·2023
    Same author

    Correction: Ankyrin-G regulates forebrain connectivity and network synchronization via interaction with GABARAP.

    Molecular psychiatry·2019
    Same author

    Ankyrin-G regulates forebrain connectivity and network synchronization via interaction with GABARAP.

    Molecular psychiatry·2018
    Same author

    Videolaryngoscopy versus direct laryngoscopy for emergency orotracheal intubation outside the operating room: a systematic review and meta-analysis.

    British journal of anaesthesia·2018

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Human erythrocytes possess a Mr 200,000 polypeptide that cross-reacts with antibodies to human platelet myosin heavy chain.
    • Immunofluorescence reveals this myosin polypeptide is present in all erythrocytes, localized punctately.

    Purpose of the Study:

    • To identify and characterize the Mr 200,000 polypeptide in human erythrocytes.
    • To investigate its localization, purification, and functional properties.

    Main Methods:

    • Immunofluorescence staining
    • Hemolysis and ghost preparation
    • DEAE-cellulose chromatography
    • Sephacryl S-400 gel filtration
    • Rotary shadowing
    • Peptide mapping
    • SDS-PAGE
    • ATPase activity assays

    Main Results:

    • The Mr 200,000 polypeptide was purified and identified as authentic vertebrate myosin.
    • Erythrocyte myosin has a heavy chain similar to platelet myosin but distinct light chains.
    • It forms bipolar filaments and exhibits ATPase activity, though not stimulated by actin.
    • Approximately 20-40% of the myosin is associated with erythrocyte membranes.

    Conclusions:

    • Human erythrocytes contain a unique myosin molecule.
    • This erythrocyte myosin is associated with the membrane cytoskeleton and may participate in an actomyosin contractile apparatus.
    • It plays a role in ATP-dependent erythrocyte shape changes.

    Related Experiment Videos