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

Partial amino acid sequence of rabbit beta2-microglobulin.

B A Cunningham, I Berggard

    Science (New York, N.Y.)
    |March 21, 1975
    PubMed
    Summary

    Researchers determined the amino acid sequence of a rabbit protein, finding it highly similar to human beta2-microglobulin. This protein also shows homology to rabbit immunoglobulin G, suggesting shared evolutionary origins.

    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

    Regulation of internodal lenght by peroxidase enzymes in grain sorghum.

    TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2014
    Same author

    Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: can solution studies define the mechanism of homophilic binding?

    Journal of molecular biology·2001
    Same author

    A short segment within the cytoplasmic domain of the neural cell adhesion molecule (N-CAM) is essential for N-CAM-induced NF-kappa B activity in astrocytes.

    Proceedings of the National Academy of Sciences of the United States of America·2001
    Same author

    Benzocaine-associated methemoglobinemia following bronchoscopy in a healthy research participant.

    Respiratory care·2000
    Same author

    N-CAM binding inhibits the proliferation of hippocampal progenitor cells and promotes their differentiation to a neuronal phenotype.

    The Journal of neuroscience : the official journal of the Society for Neuroscience·2000
    Same author

    Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM.

    FEBS letters·1999

    Area of Science:

    • Biochemistry
    • Immunology
    • Proteomics

    Background:

    • Beta2-microglobulin (B2M) is a crucial component of the Major Histocompatibility Complex (MHC) class I molecules.
    • Understanding B2M's structure and evolutionary relationships can provide insights into immune system function.
    • Low-molecular-weight proteins in urine can serve as biomarkers for various physiological and pathological conditions.

    Purpose of the Study:

    • To determine the amino acid sequence of a low-molecular-weight protein isolated from the urine of sodium dichromate-treated rabbits.
    • To compare the determined sequence with known protein sequences, particularly human beta2-microglobulin.
    • To investigate the structural and evolutionary relationship between the rabbit protein and immunoglobulin G (IgG).

    Main Methods:

    • Protein isolation from rabbit urine following sodium dichromate treatment.
    • Amino acid sequencing of the first 35 residues of the isolated protein.
    • Sequence homology analysis against human beta2-microglobulin and rabbit immunoglobulin G databases.

    Main Results:

    • The determined amino acid sequence of the rabbit protein showed identity in 30 positions with human beta2-microglobulin.
    • The rabbit protein, identified as rabbit beta2-microglobulin, exhibited significant homology to the constant regions of rabbit immunoglobulin G.
    • Specifically, the CH3 region of rabbit IgG demonstrated striking similarity to the rabbit beta2-microglobulin sequence.

    Conclusions:

    • The study successfully characterized a rabbit urinary protein as beta2-microglobulin.
    • The high sequence similarity to human beta2-microglobulin suggests conserved functional importance.
    • The homology to rabbit immunoglobulin G indicates potential shared evolutionary pathways and structural motifs between B2M and IgG.

    Related Experiment Videos