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

Stability and subunit structure of human alpha2-macroglobulin.

J P Frénoy, R Bourrillon, R Lippoldt

    The Journal of Biological Chemistry
    |February 25, 1977
    PubMed
    Summary

    Alpha2-macroglobulin

    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

    Purification of 125I-labelled lysine-vasopressin by affinity chromatography on sepharose-bound neurophysins.

    Biochimica et biophysica acta·2009
    Same author

    Active repression by thyroid hormone receptor splicing variant alpha2 requires specific regulatory elements in the context of native triiodothyronine-regulated gene promoters.

    Endocrinology·1997
    Same author

    Expression and characterization of a lactosaminoglycan-carrying glycoprotein of Zajdela hepatoma cell surface--structural analysis of the carbohydrate moiety.

    European journal of biochemistry·1997
    Same author

    Differential 9-cis-retinoic acid-dependent transcriptional activation by murine retinoid X receptor alpha (RXR alpha) and RXR beta. Role of cell type and RXR domains.

    The Journal of biological chemistry·1996
    Same author

    Structural differences between complex-type Asn-linked glycan chains of glycoproteins in rat hepatocytes and Zajdela hepatoma cells.

    Biochimica et biophysica acta·1995
    Same author

    Use of quantitative image microfluorometry to follow fluorescent ricin internalization in single living cells.

    The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society·1994

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Structural Biology

    Background:

    • Alpha2-macroglobulin (A2M) is a large plasma proteinase inhibitor.
    • Understanding its structure and stability is crucial for its biological functions.

    Purpose of the Study:

    • To determine the molecular weights and secondary structure of alpha2-macroglobulin.
    • To investigate the pH and thermal stability of alpha2-macroglobulin.

    Main Methods:

    • Equilibrium centrifugation for molecular weight determination.
    • Circular dichroism spectroscopy for secondary structure analysis.
    • Fluorescence polarization for domain size estimation.

    Main Results:

    • Molecular weights of native A2M and its subunits were determined.
    • Thermally denatured A2M exhibited a more organized polypeptide chain than the native form.
    • A2M is composed of domains smaller than its two subunits.

    Conclusions:

    • The study provides insights into the molecular weight, structure, and stability of alpha2-macroglobulin.
    • Findings contribute to understanding A2M's functional mechanisms and stability limits.

    Related Experiment Videos