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 Concept Videos

Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element.

Current biology : CB·1999
Same author

Effect of lactacidosis on cell volume and intracellular pH of astrocytes.

Journal of neurotrauma·1999
Same author

Assessment of ambulance response performance using a geographic information system.

Social science & medicine (1982)·1999
Same author

Pharmacokinetic and pharmacodynamic aspects of concomitant mibefradil-digoxin therapy at therapeutic doses.

European journal of drug metabolism and pharmacokinetics·1999
Same author

Mouse chromosome 2.

Mammalian genome : official journal of the International Mammalian Genome Society·1999
Same author

Glial cell swelling--effect of hypothermia.

Acta neurochirurgica. Supplement·1999

Related Experiment Video

Updated: Jul 28, 2026

Identification and Analysis of Mouse Erythroid Progenitors using the CD71/TER119 Flow-cytometric Assay
15:32

Identification and Analysis of Mouse Erythroid Progenitors using the CD71/TER119 Flow-cytometric Assay

Published on: August 5, 2011

Physiological variation of mouse haemoglobins.

M F Newton, J Peters

    Proceedings of the Royal Society of London. Series B, Biological Sciences
    |July 22, 1983
    PubMed
    Summary

    Genetic variations in mouse hemoglobin beta-chain (Hbb) influence oxygen transport. While Hbbd generally shows higher oxygen affinity than Hbbs, other factors likely affect survival under environmental stress.

    Area of Science:

    • Genetics
    • Physiology
    • Evolutionary Biology

    Background:

    • Polymorphism in the haemoglobin beta-chain (Hbb) gene is common in house mice (Mus musculus).
    • This genetic variation is thought to be maintained by natural selection.
    • Haemoglobin's oxygen-carrying capacity is a critical physiological attribute.

    Purpose of the Study:

    • To investigate the relationship between Hbb genotype and haemoglobin's oxygen affinity.
    • To measure P50 values in inbred mouse strains and wild populations.

    Main Methods:

    • Studied oxygen affinity by measuring P50 values.
    • Included 12 inbred mouse strains and wild-caught mice from Skokholm island.
    • Analyzed potential correlations with known oxygen binding modulators.

    More Related Videos

    Laser Doppler Perfusion Imaging in the Mouse Hindlimb
    14:45

    Laser Doppler Perfusion Imaging in the Mouse Hindlimb

    Published on: April 18, 2021

    Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
    05:08

    Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

    Published on: January 31, 2022

    Related Experiment Videos

    Last Updated: Jul 28, 2026

    Identification and Analysis of Mouse Erythroid Progenitors using the CD71/TER119 Flow-cytometric Assay
    15:32

    Identification and Analysis of Mouse Erythroid Progenitors using the CD71/TER119 Flow-cytometric Assay

    Published on: August 5, 2011

    Laser Doppler Perfusion Imaging in the Mouse Hindlimb
    14:45

    Laser Doppler Perfusion Imaging in the Mouse Hindlimb

    Published on: April 18, 2021

    Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
    05:08

    Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

    Published on: January 31, 2022

    Main Results:

    • Each inbred strain exhibited a consistent mean P50, but with significant within-strain variation.
    • Oxygen affinity fluctuated weekly in individual mice, with unclear causes.
    • Mice homozygous for Hbbd generally showed higher oxygen affinity than those homozygous for Hbbs.

    Conclusions:

    • Haemoglobin oxygen dissociation properties alone may not solely determine the survival advantage of specific Hbb types.
    • Environmental stress likely interacts with multiple factors, including haemoglobin function, to influence differential survival.
    • Further research is needed to elucidate the causes of within-individual variation in oxygen affinity.