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 subunit structure of thyroglobulin

R Pitt-Rivers

    The Biochemical Journal
    |September 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Researchers reduced and alkylated human and rat thyroglobulin, finding the resulting molecules had a molecular weight of approximately 165,000, a quarter of the original size.

    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

    The effects of drugs on the distribution and metabolism of thyroid hormones.

    Pharmacological reviews·1981
    Same author

    Charles Robert Harington, 1897-1972.

    Biographical memoirs of fellows of the Royal Society. Royal Society (Great Britain)·1972
    Same author

    Synthesis of a radioiodine-labeled 2,4-dinitrophenyl-hapten and its use for binding assays.

    European journal of immunology·1971
    Same author

    Radioautographic studies of the initial site of formation of protein-bound iodine in the rat thyroid gland.

    The Biochemical journal·1970
    Same author

    The subunits of thyroglobulin.

    The Biochemical journal·1970
    Same author

    The binding of sodium dodecyl sulphate to various proteins.

    The Biochemical journal·1968

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Thyroglobulin is a large glycoprotein essential for thyroid hormone synthesis.
    • Understanding thyroglobulin's structure is crucial for comprehending thyroid function and related disorders.

    Purpose of the Study:

    • To investigate the molecular weight changes of thyroglobulin after reduction and alkylation.
    • To determine if the reduction and alkylation process affects thyroglobulin from different species (human and rat) similarly.

    Main Methods:

    • Human and rat thyroglobulin were subjected to reduction and alkylation.
    • These reactions were performed under aqueous alkaline conditions without denaturants.
    • The molecular weight of the resulting product was analyzed.

    Related Experiment Videos

    Main Results:

    • The reduction and alkylation of both human and rat thyroglobulin yielded a product with a molecular weight of approximately 165,000.
    • This molecular weight represents one-quarter of the molecular weight of the native, unreduced thyroglobulin molecule.

    Conclusions:

    • Reduction and alkylation significantly reduce the molecular weight of thyroglobulin, suggesting the dissociation of subunits.
    • The observed molecular weight reduction is consistent across both human and rat thyroglobulin, indicating conserved structural properties related to disulfide bonds.