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

Proteolytic activity in developing bovine enamel.

D Moe, H Birkedal-Hansen

    Journal of Dental Research
    |March 1, 1979
    PubMed
    Summary

    Enamel matrix from bovine teeth contains a serine protease that degrades enamel proteins. This enzyme shows optimal activity at pH 8-9, aiding in understanding tooth 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

    Individual variations in protective effects of experimentally formed salivary pellicles.

    Caries research·2009
    Same author

    Optimal drinking water composition for caries control in populations.

    Journal of dental research·2008
    Same author

    Analyses of Pseudomonas aeruginosa lectin binding to alpha-galactosylated glycans.

    Current microbiology·2005
    Same author

    The effect of spironolactone on experimental periodontitis in rats.

    Journal of periodontal research·2005
    Same author

    Effect of saliva composition on experimental root caries.

    Caries research·2004
    Same author

    Inhibition of molar eruption and root elongation in MT1-MMP-deficient mice.

    Connective tissue research·2003

    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Enamel Matrix Research

    Background:

    • Tooth enamel formation involves complex protein matrix degradation.
    • Understanding the enzymes responsible for matrix remodeling is crucial for developmental biology.

    Purpose of the Study:

    • To identify and characterize proteolytic activity within partially mineralized enamel matrix.
    • To determine the optimal conditions and enzyme class responsible for enamel matrix protein degradation.

    Main Methods:

    • Extraction of partially mineralized enamel matrix from bovine incisor tooth germs.
    • Assay of proteolytic activity using enamel matrix proteins, casein, and azocoll.
    • Enzyme inhibition studies to identify the protease family.

    Main Results:

    • Proteolytic activity was detected in the enamel matrix, capable of degrading enamel matrix proteins.
    • Optimal protease activity occurred at neutral to slightly alkaline pH (8-9).
    • Inhibitor studies identified the enzyme as a serine protease belonging to the chymotrypsin family.

    Conclusions:

    • A chymotrypsin-like serine protease is present in developing bovine enamel.
    • This enzyme plays a role in the degradation of enamel matrix proteins during tooth development.
    • Further research can explore this protease's function in amelogenesis.

    Related Experiment Videos