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

A superactive insulin: [B10-aspartic acid]insulin(human).

G P Schwartz, G T Burke, P G Katsoyannis

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1987
    PubMed
    Summary

    A single genetic mutation in the proinsulin gene creates a superactive insulin analogue, [AspB10]insulin. This enhanced hormone exhibits significantly higher binding affinity and potency, offering insights into insulin receptor interactions.

    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

    A Case of Gumma of the Vertebræ.

    The Indian medical gazette·2017
    Same author

    A Case of Tabes Dorsalis in an Indian.

    The Indian medical gazette·2017
    Same author

    A Case of Fibro-Lipomatosis Associated with Fever.

    The Indian medical gazette·2017
    Same author

    Chronic Amœbic Infection as a Cause of Ill-Health.

    The Indian medical gazette·2017
    Same author

    A Case of Malaria with Cerebellar Localization.

    The Indian medical gazette·2017
    Same author

    An Unusual Case of Jaundice Associated with Hodgkin's Disease.

    The Indian medical gazette·2017

    Area of Science:

    • Biochemistry
    • Genetics
    • Endocrinology

    Background:

    • Familial hyperproinsulinemia is a genetic disorder.
    • A recent study identified a single point mutation in the proinsulin gene causing this condition.
    • The mutation results in the substitution of histidine-10 with aspartic acid in the B chain of insulin.

    Purpose of the Study:

    • To synthesize and evaluate the biological activity of a human insulin analogue, [AspB10]insulin, corresponding to the identified mutation.
    • To investigate the impact of this specific amino acid substitution on insulin's interaction with its receptor and its overall potency.

    Main Methods:

    • Synthesis of the [AspB10]insulin analogue.
    • Assessment of binding affinity to insulin receptors using rat liver plasma membranes.

    Related Experiment Videos

  • Evaluation of biological potency through lipogenesis assays.
  • Analysis of physicochemical properties using reversed-phase High-Performance Liquid Chromatography (HPLC).

    • Main Results:

    • The [AspB10]insulin analogue demonstrated a 534% relative binding affinity to insulin receptors compared to natural insulin.
    • The synthetic analogue showed a 435% relative potency in lipogenesis assays, comparable to its binding affinity.
    • Reversed-phase HPLC revealed that [AspB10]insulin is more apolar than natural insulin.

    Conclusions:

    • A single amino acid substitution (Aspartic acid for Histidine-10) in human insulin results in a superactive hormone.
    • The enhanced properties of [AspB10]insulin are attributed to conformational changes leading to stronger insulin receptor interaction.
    • This finding provides valuable insights into structure-activity relationships of insulin and receptor binding.