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

Onconase: an unusually stable protein.

E Notomista1, F Catanzano, G Graziano

  • 1Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Via Mezzocannone 16, 80134 Naples, Italy.

Biochemistry
|July 29, 2000
PubMed
Summary

Onconase, a small antitumor enzyme, exhibits remarkable stability and low catalytic activity. This study explores the molecular basis for its stability and low activity, crucial for its drug development.

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

<i>Trichinella</i> surveillance program in wild birds, Emilia-Romagna (northern Italy), 2006-2021. First report of <i>Trichinella pseudospiralis</i> in western marsh harrier (<i>Circus aeruginosus</i>) in Italy.

International journal for parasitology. Parasites and wildlife·2022
Same author

Transcriptomic and genomic analysis provides new insights in molecular and genetic processes involved in zucchini ZYMV tolerance.

BMC genomics·2022
Same author

The plant diterpene epoxysiderol targets Hsp70 in cancer cells, affecting its ATPase activity and reducing its translocation to plasma membrane.

International journal of biological macromolecules·2021
Same author

Search for Heavy Resonances Decaying into a Photon and a Hadronically Decaying Higgs Boson in pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2021
Same author

Migration of the femoral component and clinical outcomes after total knee replacement: a narrative review.

Musculoskeletal surgery·2020
Same author

Search for Higgs Boson Decays into a Z Boson and a Light Hadronically Decaying Resonance Using 13 TeV pp Collision Data from the ATLAS Detector.

Physical review letters·2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • The RNase A superfamily contains enzymes with antitumor properties.
  • Onconase, a small RNase A member, shows selective cytotoxicity and is in phase-III clinical trials.
  • Onconase possesses unusual stability, low catalytic activity, and potential renal toxicity.

Purpose of the Study:

  • To investigate the molecular determinants of onconase stability and low catalytic activity.
  • To compare the stability and proteolysis sensitivity of onconase and its catalytically active mutant (M23L)-ONC.
  • To develop a model explaining onconase's stability and low activity.

Main Methods:

  • Differential scanning calorimetry
  • Circular dichroism

Related Experiment Videos

  • Fluorescence spectroscopy
  • Limited proteolysis
  • Thermodynamic parameter determination

    • Main Results:

    • Onconase is an unusually stable protein, confirmed by its resistance to proteolysis.
    • (M23L)-ONC mutant is less stable and more sensitive to proteolysis than wild-type onconase.
    • Thermodynamic analysis revealed key parameters contributing to onconase's stability.

    Conclusions:

    • Onconase's high stability is a key characteristic, potentially linked to its low catalytic activity.
    • A model was constructed explaining the molecular basis of onconase stability and low activity.
    • Understanding these properties is vital for onconase's therapeutic application.