Jove
Visualize
Contact Us

Related Experiment Videos

Endoplasmic reticulum nuclease. Purification and specificity.

S Kouidou, A Triantos, E Kavoukopoulos

    European Journal of Biochemistry
    |November 1, 1981
    PubMed
    Summary

    This study isolated an endonuclease from rat liver endoplasmic reticulum with significant RNase activity. The enzyme is oligomeric, binds nucleotides, and preferentially degrades RNA, offering insights into nucleic acid metabolism.

    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

    Risk-associated coding synonymous SNPs in type 2 diabetes and neurodegenerative diseases: genetic silence and the underrated association with splicing regulation and epigenetics.

    Mutation research·2015
    Same author

    Drugs of abuse: epigenetic mechanisms in toxicity and addiction.

    Current medicinal chemistry·2011
    Same author

    Epigenetically-targeted therapies for the treatment of hematological malignancies.

    Current medicinal chemistry·2011
    Same author

    Frequent presence of incomplete HPV16 E7 ORFs in lung carcinomas: memories of viral infection.

    Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology·2010
    Same author

    DNA repair enables sex identification in genetic material from human teeth.

    Hippokratia·2009
    Same author

    Effects of a low-calorie diet associated with weight loss on lipoprotein-associated phospholipase A2 (Lp-PLA2) activity in healthy obese women.

    Nutrition, metabolism, and cardiovascular diseases : NMCD·2007
    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

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Endonucleases play crucial roles in nucleic acid metabolism and regulation.
    • Rat liver endoplasmic reticulum is a key cellular compartment for protein and lipid synthesis, and thus a potential source of regulatory enzymes.

    Purpose of the Study:

    • To isolate and characterize an endonuclease from rat liver endoplasmic reticulum.
    • To investigate the enzyme's enzymatic activities, substrate specificities, and structural properties.

    Main Methods:

    • Enzyme isolation and purification using gel chromatography.
    • Molecular weight determination via gel chromatography and SDS-PAGE.
    • Nucleolytic activity assays using various nucleic acid substrates.
    • Nucleotide binding studies.

    Related Experiment Videos

    Main Results:

    • Isolation of an oligomeric endonuclease from rat liver endoplasmic reticulum with four active fractions of varying molecular weights.
    • Subunits of the enzyme share similar molecular weights (Mr 5.4 X 10(4)).
    • The enzyme exhibits primarily RNase activity, with limited degradation of denatured DNA and DNA.RNA hybrids.
    • Poly(A) and Poly(U) are the most susceptible RNA substrates, while Poly(C) is resistant.
    • Deoxyribonucleoside and ribonucleoside triphosphates can bind to the nuclease, enhanced by Mg2+.

    Conclusions:

    • The characterized endonuclease is an oligomeric protein with predominant RNase activity.
    • Its ability to bind nucleotides suggests a potential regulatory role in nucleic acid metabolism.
    • The differential susceptibility of RNA homopolymers indicates specific recognition mechanisms.