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

Differences between human and rabbit transferrins.

J V Princiotto, E J Zapolski

    Biochimica Et Biophysica Acta
    |February 13, 1978
    PubMed
    Summary
    This summary is machine-generated.

    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

    On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: II. Peptide sequence analysis.

    Electrophoresis·1991
    Same author

    A system for automated DNA electrophoresis, molecular hybridization and electronic detection: II. Electronic detection.

    Electrophoresis·1989
    Same author

    Rapid polyacrylamide slab drying using a microwave gel dryer.

    Analytical biochemistry·1983
    Same author

    Computer applications in analysis, mapping and cataloging of proteins separated by two dimensional electrophoresis.

    Computers in biology and medicine·1983
    Same author

    The demonstration of alpha 1 antitrypsin in periapical lesions.

    Oral surgery, oral medicine, and oral pathology·1983
    Same author

    [59Fe]Ferrous bathophenanthroline sulfonate: a radioactive stain for labeling proteins in situ in polyacrylamide gels.

    Analytical biochemistry·1982
    Same journal

    Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Molecular Basis of Disease Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    General Subjects Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

    Biochimica et biophysica acta·2019
    Same journal

    Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

    Biochimica et biophysica acta·2019
    Same journal

    Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

    Biochimica et biophysica acta·2019
    See all related articles

    Rabbit and human transferrin exhibit distinct iron-binding behaviors. Rabbit transferrin is functionally homogeneous, while human transferrin shows unique iron-binding properties, impacting iron uptake by reticulocytes.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Hematology

    Background:

    • Transferrin is the primary iron transport protein in serum.
    • Iron uptake by cells, particularly reticulocytes, is crucial for erythropoiesis.
    • Differences in transferrin structure and function can influence iron bioavailability.

    Purpose of the Study:

    • To investigate the mechanism of iron incorporation from rabbit transferrin into rabbit reticulocytes.
    • To compare the iron-binding properties of rabbit transferrin with human transferrin.
    • To elucidate the role of transferrin iron saturation and pH in iron uptake.

    Main Methods:

    • Experiments using rabbit reticulocytes and radiolabeled iron.
    • Incubation of reticulocytes with varying concentrations of rabbit and human transferrin.

    Related Experiment Videos

  • Analysis of iron incorporation rates under different pH conditions.

    • Main Results:

    • Iron incorporation from rabbit transferrin into rabbit reticulocytes was independent of transferrin iron saturation.
    • Iron uptake from human transferrin into rabbit reticulocytes was dependent on transferrin iron saturation.
    • Rabbit transferrin demonstrated functional homogeneity in iron release, unlike human transferrin, and lacked acid-pH iron-binding capabilities.

    Conclusions:

    • Rabbit transferrin exhibits unique iron-binding and release characteristics compared to human transferrin.
    • These differences influence the regulation of iron uptake by reticulocytes.
    • The findings highlight species-specific mechanisms in iron transport and metabolism.