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 membrane-bound basic carboxypeptidase from hog intestinal mucosa(1).

F Dalle Ore1, E H Ajandouz, T Giardina

  • 1Laboratoire de Biochimie et Biologie de la Nutrition, CNRS-ESA 6033, Faculté des Sciences et Techniques de Saint-Jérôme, 13 397, Marseille, France.

Biochimica Et Biophysica Acta
|October 16, 1999
PubMed
Summary

Hog intestinal mucosa contains two distinct carboxypeptidases. One is membrane-bound with neutral pH optimum, while the other is soluble with acidic pH optimum, potentially cathepsin B.

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

Ruminococcus gnavus E1 modulates mucin expression and intestinal glycosylation.

Journal of applied microbiology·2016
Same author

Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont.

Applied and environmental microbiology·2012
Same author

Intron retention regulates the expression of pectin methyl esterase inhibitor (Pmei) genes during wheat growth and development.

Plant biology (Stuttgart, Germany)·2011
Same author

Ruminococcin C, a new anti-Clostridium perfringens bacteriocin produced in the gut by the commensal bacterium Ruminococcus gnavus E1.

Biochimie·2011
Same author

Inhibition of porcine liver carboxylesterase by a new flavone glucoside isolated from Deverra scoparia.

Chemico-biological interactions·2008
Same author

Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease.

FEBS letters·2006

Area of Science:

  • Biochemistry
  • Enzymology
  • Gastrointestinal Physiology

Background:

  • Hog intestinal mucosa exhibits carboxypeptidase activity, crucial for releasing COOH-terminal amino acids from peptides.
  • This activity is attributed to at least two distinct enzymes with differing properties.
  • Understanding these enzymes aids in elucidating digestive processes and potential therapeutic targets.

Purpose of the Study:

  • To characterize the distinct carboxypeptidase activities in hog intestinal mucosa.
  • To differentiate between the membrane-bound and soluble enzyme forms.
  • To compare the hog intestinal enzymes with human placental carboxypeptidase M.

Main Methods:

  • Enzyme activity assays at varying pH levels and in the presence of specific inhibitors (CoCl2, guanidinoethylmercaptosuccinic acid, o-phenanthroline, EDTA, cadmium acetate, NiCl2).

Related Experiment Videos

  • Solubilization studies using phosphatidylinositol-specific phospholipase C and detergents.
  • Molecular mass determination via SDS-PAGE and gel filtration; immunoblotting analysis.

    • Main Results:

    • Two distinct carboxypeptidase activities were identified: a membrane-bound enzyme with neutral pH optimum and a soluble enzyme with acidic pH optimum (likely cathepsin B).
    • The membrane-bound enzyme was enhanced by CoCl2 and inhibited by specific agents, unlike the soluble form.
    • The purified membrane-bound enzyme (200 kDa) differs significantly in molecular mass and substrate specificity (cleaves lysyl bonds faster than arginyl bonds) from human carboxypeptidase M (62 kDa).

    Conclusions:

    • Hog intestinal mucosa possesses at least two distinct carboxypeptidases, a membrane-bound form and a soluble form.
    • The membrane-bound enzyme is a large glycoprotein, distinct from human carboxypeptidase M.
    • The hog intestinal membrane-bound carboxypeptidase is proposed to be carboxypeptidase D.