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

Hemoglobin variants with altered oxygen affinity

R T Jones, T B Shih

    Hemoglobin
    |January 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    Abnormal hemoglobins alter oxygen affinity, impacting red blood cell oxygen levels. Specific structural changes reveal how these hemoglobin variants affect oxygen binding and related health conditions.

    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

    Upper Limit on the Photoproduction Cross Section of the Spin-Exotic π_{1}(1600).

    Physical review letters·2025
    Same author

    Precision Measurement of the Beam-Normal Single-Spin Asymmetry in Forward-Angle Elastic Electron-Proton Scattering.

    Physical review letters·2020
    Same author

    First Measurement of Near-Threshold J/ψ Exclusive Photoproduction off the Proton.

    Physical review letters·2019
    Same author

    Heavy metal pollution and co-selection for antibiotic resistance: A microbial palaeontology approach.

    Environment international·2019
    Same author

    Preferential reduction of synaptic efficacy in the dentate gyrus of hippocampal slices from aged rats during reduced glucose availability.

    Neuroscience·2015
    Same author

    Orientation and conformation of anti-CD34 antibody immobilised on untreated and plasma treated polycarbonate.

    Acta biomaterialia·2015
    Same journal

    Compound Heterozygous Hemoglobin Minneapolis-Laos and Codon 41/42 (-TTCT) in a Thai Female Adult: A Case Report and Literature Review.

    Hemoglobin·2026
    Same journal

    Hb F-SickKids (<i>HBG2</i>: C.308A > G): A Novel γ-Globin Variant Associated with Transient Neonatal Cyanosis.

    Hemoglobin·2026
    Same journal

    Pyruvate Kinase Activation in the Management of Thalassemia and Sickle Cell Disease.

    Hemoglobin·2026
    Same journal

    Genotypic Characterization of Hemoglobinopathies in Azerbaijan: A Review of 10 Years at a Referral Center.

    Hemoglobin·2026
    Same journal

    Successful Management of Transfusion-Dependent Unstable Hemoglobin Perth with Splenectomy: First Report from Iran and Literature Review.

    Hemoglobin·2026
    Same journal

    Unstable Hemoglobin Variants: Molecular Mechanisms, Clinical Phenotypes, and a Practical Diagnostic and Management Approach.

    Hemoglobin·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Hematology

    Background:

    • 88 abnormal hemoglobins with altered oxygen affinities are known.
    • These variants include high-affinity (60) and low-affinity (28) types, with 26 being chemically unstable.

    Purpose of the Study:

    • To classify hemoglobin variants based on structural changes.
    • To understand the structure-function relationship of abnormal hemoglobins and their impact on oxygen affinity.

    Main Methods:

    • Classification of hemoglobin variants by amino acid changes at specific structural sites (e.g., subunit interfaces, heme contacts, DPG binding site).
    • Functional studies of six abnormal hemoglobins at critical residue positions.

    Main Results:

    Related Experiment Videos

  • High-affinity variants are linked to erythrocytosis or normal red cell mass.
  • Low-affinity variants can cause anemia, potentially due to chemical instability.
  • A correlation exists between P50 values and hemoglobin concentration in stable variants.

    • Conclusions:

    • Hemoglobin-oxygen affinity is critically dependent on specific residue alterations and substituted group properties.
    • Comparative studies of variants at the same position offer insights into oxygen binding mechanisms.