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

The multicatalytic proteinase. Multiple proteolytic activities.

A J Rivett1

  • 1Department of Biochemistry, University of Leicester, United Kingdom.

The Journal of Biological Chemistry
|July 25, 1989
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

Regulation of proteasome complexes by gamma-interferon and phosphorylation.

Biochimie·2001
Same author

Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer.

EMBO reports·2001
Same author

gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation.

The Biochemical journal·2001
Same author

Association of immunoproteasomes with the endoplasmic reticulum.

The Biochemical journal·2000
Same author

Proteasome inhibitors: from in vitro uses to clinical trials.

Journal of peptide science : an official publication of the European Peptide Society·2000
Same author

Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells.

The Biochemical journal·2000
Same journal

Wanted and unwanted modifications of mRNA, and their effect on gene expression and signaling.

The Journal of biological chemistry·2026
Same journal

TGF-β2 drives lipid droplet accumulation in chondrocytes through the TβRI/p-Smad3/Fabp5 axis.

The Journal of biological chemistry·2026
Same journal

Macrophage-specific targeting of histone demethylases with small-molecule inhibitors suppresses inflammatory response in vivo.

The Journal of biological chemistry·2026
Same journal

Substrate and target selectivity of 4'-fluoroadenosine against viral and host polymerases.

The Journal of biological chemistry·2026
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
See all related articles

The multicatalytic proteinase, found in mammalian tissues, exhibits distinct trypsin-like and chymotrypsin-like activities. These proteolytic functions are linked to a single enzyme complex, suggesting multiple catalytic sites within one protein.

Area of Science:

  • Biochemistry
  • Enzymology
  • Proteomics

Background:

  • The multicatalytic proteinase is a high molecular weight, nonlysosomal enzyme found in various mammalian tissues.
  • This proteinase is known to degrade protein and peptide substrates, cleaving bonds adjacent to basic, hydrophobic, and acidic amino acid residues.

Purpose of the Study:

  • To investigate the distinct catalytic activities within the multicatalytic proteinase.
  • To determine if multiple catalytic sites exist within the single protein complex.

Main Methods:

  • Utilizing synthetic peptide substrates to differentiate enzyme activities.
  • Employing specific inhibitors (leupeptin, antipain, N-ethylmaleimide) to assess trypsin-like and chymotrypsin-like activities.
  • Conducting mixed-substrate experiments and antibody-based assays.

Related Experiment Videos

Main Results:

  • The multicatalytic proteinase displays trypsin-like and chymotrypsin-like activities, alongside peptidyl-glutamyl peptide bond hydrolysis.
  • Distinct catalytic sites were suggested by differential inhibition patterns and mixed-substrate experiments.
  • All proteolytic activities were lost upon dissociation of the protein complex.

Conclusions:

  • The multicatalytic proteinase possesses at least two distinct catalytic sites within a single complex.
  • The enzyme's multiple proteolytic activities are associated with a single protein band on native polyacrylamide gels.
  • Further research is needed to fully elucidate the structure-function relationship of this complex enzyme.