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

Acylpeptide hydrolase activity from erythrocytes.

W M Jones, J M Manning

    Biochemical and Biophysical Research Communications
    |January 31, 1985
    PubMed
    Summary

    Human erythrocytes contain purified acylpeptide hydrolase, an enzyme that removes blocked amino acids from peptides. This enzyme shows varied pH optima and is inhibited by zinc, suggesting a role in polypeptide processing during biosynthesis.

    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

    [2] Determination of d- and l-amino acids by ion-exchange chromatography.

    Methods in enzymology·2012
    Same author

    Allergen-specific sublingual immunotherapy in the treatment of migraines: a prospective study.

    European review for medical and pharmacological sciences·2011
    Same author

    Case of Pleuritic Effusion: Paracentes is Three Times: Death: Necropsy.

    British medical journal·2010
    Same author

    A methyl methacrylate-silica replica technique for electron microscopy.

    Nature·2010
    Same author

    Relationships between rigging set-up, anthropometry, physical capacity, rowing kinematics and rowing performance.

    Sports biomechanics·2004
    Same author

    Adherence of vancomycin to proteins.

    Journal of protein chemistry·2002

    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Acylpeptide hydrolase is an enzyme responsible for cleaving N-terminal blocked amino acids from peptides.
    • Understanding the properties and function of this enzyme is crucial for insights into protein processing.
    • Human erythrocytes serve as a source for studying enzymes involved in cellular metabolism.

    Purpose of the Study:

    • To purify acylpeptide hydrolase from human erythrocytes.
    • To characterize the substrate specificity and kinetic properties of the purified enzyme.
    • To investigate the potential role of acylpeptide hydrolase in polypeptide biosynthesis.

    Main Methods:

    • Purification of acylpeptide hydrolase to apparent homogeneity from human erythrocytes.
    • Enzyme activity assays using diverse peptide substrates.
    • Determination of pH optima for substrate hydrolysis.
    • Assessment of the effect of zinc on enzyme activity.

    Main Results:

    • Acylpeptide hydrolase was successfully purified to homogeneity from human erythrocytes.
    • The enzyme demonstrated hydrolysis of a wide range of peptide substrates.
    • Different pH optima were observed for the hydrolysis of various substrates.
    • Zinc was found to inhibit the hydrolysis of both efficient and inefficient substrates uniformly.

    Conclusions:

    • The purified acylpeptide hydrolase from human erythrocytes possesses broad substrate specificity and distinct kinetic properties.
    • The enzyme's activity is modulated by pH and inhibited by zinc.
    • Acylpeptide hydrolase may play a significant role in the post-translational modification and processing of polypeptide chains during biosynthesis.

    Related Experiment Videos