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

Bovine trypsinogen activation. A thermodynamic study.

M Coletta1, P Ascenzi, G Amiconi

  • 1Department of Biochemical Sciences, University of Rome La Sapienza, Italy.

Biophysical Chemistry
|August 31, 1990
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

Human collecting lymphatic glycocalyx identification by electron microscopy and immunohistochemistry.

Scientific reports·2023
Same author

POR polymorphisms are associated with 21 hydroxylase deficiency.

Journal of endocrinological investigation·2021
Same author

Safety of outpatient percutaneous native renal biopsy in systemic autoimmune diseases: results from a monocentric cohort.

Lupus·2018
Same author

Investigation of cerebral venous outflow in microgravity.

Physiological measurement·2017
Same author

Lower Limbs Venous Kinetics and Consequent Impact on Drainage Direction.

Journal of vascular surgery. Venous and lymphatic disorders·2016
Same author

Oscillatory Turbulent Flow in Chronic Venous Disease Induces Pro-inflammatory and Reparative Biological Signaling.

Journal of vascular surgery. Venous and lymphatic disorders·2016

The N-alpha-L-isoleucyl-L-valine (Ile-Val) dipeptide activates bovine trypsinogen by influencing ligand binding. This study explores the thermodynamics of this activation and ligand interactions with bovine trypsinogen and beta-trypsin.

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Chemistry

Background:

  • Bovine trypsinogen activation involves specific N-terminal sequences.
  • Dipeptides can modulate enzyme activity and ligand binding.
  • Understanding trypsinogen activation is crucial for protease research.

Purpose of the Study:

  • Investigate the activating effect of the N-alpha-L-isoleucyl-L-valine (Ile-Val) dipeptide on bovine trypsinogen.
  • Determine the thermodynamics of ligand interactions with bovine trypsinogen and beta-trypsin.
  • Elucidate the linkage relationships governing interactions within the trypsinogen system.

Main Methods:

  • Enzyme kinetics studies at varying pH (3.0-9.0) and temperature (21.0°C).
  • Thermodynamic analysis of ligand binding equilibria.

Related Experiment Videos

  • Characterization of interactions between dipeptides, inhibitors, and bovine trypsinogen/beta-trypsin.

    • Main Results:

    • The Ile-Val dipeptide demonstrated an activating effect on ligand binding equilibria for bovine trypsinogen.
    • Thermodynamic parameters for strong ligand interactions (n-butylamine, PSTI) with bovine beta-trypsin were determined.
    • Linkage relationships revealed complex interactions between functional domains of the enzyme and its zymogen.

    Conclusions:

    • The Ile-Val dipeptide plays a significant role in modulating bovine trypsinogen activation.
    • Interactions between the Ile-Val pocket and recognition subsites are critical for the activation pathway.
    • This research provides insights into the intricate molecular mechanisms of trypsinogen activation and regulation.