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 alpha-2-macroglobulin. Studies on the electrophoretic heterogeneity.

L P Nelles, P K Hall, R C Roberts

    Biochimica Et Biophysica Acta
    |May 29, 1980
    PubMed
    Summary

    Alpha-2-macroglobulin exhibits microheterogeneity due to conformational changes, not degradation. These different forms impact its proteinase binding capacity, crucial for understanding its 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

    Estrogen-related receptor gamma regulates mitochondrial and synaptic genes and modulates vulnerability to synucleinopathy.

    NPJ Parkinson's disease·2022
    Same author

    Direct microfabrication of oxide patterns by local electrodeposition of precisely positioned electrolyte: the case of Cu2O.

    Scientific reports·2016
    Same author

    Decreased synaptic and mitochondrial density in the postmortem anterior cingulate cortex in schizophrenia.

    Schizophrenia research·2015
    Same author

    Localization of excitatory amino acid transporters EAAT1 and EAAT2 in human postmortem cortex: a light and electron microscopic study.

    Neuroscience·2014
    Same author

    Ultrastructural localization of tyrosine hydroxylase in tree shrew nucleus accumbens core and shell.

    Neuroscience·2014
    Same author

    Selection for efficiency of feed utilization in growing mice.

    TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2013

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Proteomics

    Background:

    • Alpha-2-macroglobulin (A2M) is a major human protease inhibitor.
    • Its functional integrity is critical for regulating proteolytic processes.
    • Microheterogeneity in A2M preparations can complicate functional studies.

    Purpose of the Study:

    • To investigate the nature of electrophoretic microheterogeneity in purified alpha-2-macroglobulin.
    • To determine the relationship between different electrophoretic forms and proteinase binding capacity.
    • To assess potential differences in A2M from cystic fibrosis plasma.

    Main Methods:

    • Polyacrylamide gel electrophoresis (PAGE) to resolve A2M.
    • Zymogram techniques to assess proteinase binding post-electrophoresis.

    Related Experiment Videos

  • Mild alkaline treatment to study subunit cleavage.
  • Comparison of A2M from cystic fibrosis and control plasma.

    • Main Results:

    • Purified A2M resolves into multiple electrophoretic bands, reflecting conformational states, not proteolytic damage.
    • Fast electrophoretic forms exhibit significantly lower trypsin binding capacity compared to slower forms.
    • No electrophoretic differences were observed between A2M from cystic fibrosis and control plasma.
    • A2M converts from a slow to faster forms during plasma aging or purification.

    Conclusions:

    • Electrophoretic microheterogeneity of alpha-2-macroglobulin is attributed to conformational variations.
    • The proportion of different electrophoretic forms directly influences proteinase binding capacity.
    • Characterizing A2M's electrophoretic heterogeneity is essential before studying its proteinase binding properties.
    • A2M from cystic fibrosis plasma does not show distinct electrophoretic profiles compared to controls.