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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
    This summary is machine-generated.

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    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.

    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.

    Related Experiment Videos

  • 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.