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

Is elastomucoproteinase a double-headed enzyme?

G Cs-Szabó, E Gyáni, I Banga

    Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae
    |January 1, 1985
    PubMed
    Summary

    Elastomucoproteinase (EMPase), found with pancreatic elastase, shows both protein-degrading and mucus-thinning abilities. These dual activities may stem from separate enzyme sites, offering new insights into protease function.

    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

    Characterization of degenerative human facet joints and facet joint capsular tissues.

    Osteoarthritis and cartilage·2015
    Same author

    Splitting of adenosine triphosphate by myosin.

    Nature·2010
    Same author

    Nature of myosin.

    Nature·2010
    Same author

    TGF beta 1 and biglycan, decorin, and fibromodulin metabolism in canine cartilage.

    Osteoarthritis and cartilage·2003
    Same author

    The effects of collagen fragments on the extracellular matrix metabolism of bovine and human chondrocytes.

    Connective tissue research·2001
    Same author

    Human articular chondrocytes express osteogenic protein-1.

    The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society·2000

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Pancreatic elastase isolation often yields a minor component, elastomucoproteinase (EMPase).
    • EMPase possesses dual proteolytic and mucolytic activities.

    Purpose of the Study:

    • To characterize the enzymatic properties of EMPase.
    • To investigate the nature of its proteolytic and mucolytic activities.

    Main Methods:

    • Anion-exchange chromatography for EMPase purification.
    • Substrate assays using aortic preparations and tripeptide-p-nitroanilides.
    • Enzyme inhibition studies with phenylmethanesulphonyl fluoride.
    • SDS-gel electrophoresis to determine subunit composition.

    Main Results:

    • EMPase cleaves carbohydrate moieties and peptide bonds in aortic preparations.
    • Proteolytic activity is specific for substrates with C-terminal Phe or Tyr.
    • Bz-Ala-Gly-Phe-pNA showed best binding, Bz-Ala-Pro-Tyr-pNA fastest hydrolysis.
    • Phenylmethanesulphonyl fluoride completely inhibited proteolytic activity but only 20% of mucolytic activity.
    • SDS-PAGE indicated EMPase is a single polypeptide chain.

    Conclusions:

    • EMPase exhibits distinct proteolytic and mucolytic functions.
    • These activities likely reside in separate enzyme sites.
    • EMPase is a single polypeptide chain enzyme.

    Related Experiment Videos