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

Subunit dissociation in fish hemoglobins.

S J Edelstein, B McEwen, Q H Gibson

    The Journal of Biological Chemistry
    |December 10, 1976
    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

    Passivation of acceptors in GaN by hydrogen and their activation.

    Nanotechnology·2024
    Same author

    An evaluation of the need of the long-stay psychiatric patient for organised exercise.

    The Australian journal of physiotherapy·2014
    Same author

    Commentary: the role of the toxicologic pathologist in academia.

    Veterinary pathology·2014
    Same author

    The association between submission counts to a veterinary diagnostic laboratory and the economic and disease challenges of the Ontario swine industry from 1998 to 2009.

    Preventive veterinary medicine·2012
    Same author

    Concentration of lipocalin region of collagen XXVII alpha 1 in the serum of dogs with hemangiosarcoma.

    Journal of veterinary internal medicine·2011
    Same author

    The ratios of iron to oxygen, iron to colour and oxygen to colour in the blood of men and women.

    The Journal of physiology·2010

    Fish hemoglobins exhibit lower tetramer-dimer dissociation than mammalian hemoglobins. Their equilibrium constants (K 4,2) are intermediate between liganded and unliganded human hemoglobin, indicating greater stability in tetrameric form.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Comparative Physiology

    Background:

    • Hemoglobin (Hb) exists as tetramers and dimers, with dissociation influenced by ligand binding and environmental factors.
    • Understanding Hb quaternary structure dynamics is crucial for elucidating oxygen transport mechanisms across species.

    Purpose of the Study:

    • To investigate the tetramer-dimer dissociation equilibria (K 4,2) of fish hemoglobins.
    • To compare the dissociation behavior of fish hemoglobins with mammalian hemoglobins.

    Main Methods:

    • Sedimentation velocity measurements using ultracentrifugation with scanner-computer system.
    • Flash photolysis experiments employing rapid kinetic methods.
    • Analysis of dissociation in the presence of denaturants like guanidine hydrochloride and urea.

    Related Experiment Videos

    Main Results:

    • Fish hemoglobins (menhaden, carp, blue shark) showed minimal dissociation in 0.1 M phosphate buffer (pH 7), suggesting K 4,2 ≤ 10(-8) M.
    • Flash photolysis revealed K 4,2 values in the range of 10(-9) to 10(-8) M for liganded fish hemoglobins.
    • Fish Hb dissociation in guanidine hydrochloride (0.8 M) was intermediate between liganded (0.4 M) and unliganded (1.6 M) human Hb.

    Conclusions:

    • Fish hemoglobins exhibit greater stability in their tetrameric form compared to mammalian hemoglobins.
    • The K 4,2 values for liganded fish hemoglobins are intermediate between those of liganded and unliganded human hemoglobin.
    • These findings highlight evolutionary adaptations in hemoglobin structure and function across different vertebrate classes.