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

Phosphofructokinase is a calmodulin binding protein.

G W Mayr, L M Heilmeyer

    FEBS Letters
    |August 8, 1983
    PubMed
    Summary
    This summary is machine-generated.

    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

    Reduced proliferation of CD34(+) cells from patients with acute myeloid leukemia after gene transfer of INPP5D.

    Gene therapy·2009
    Same author

    Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations.

    Gene therapy·2007
    Same author

    Restoration of SHIP activity in a human leukemia cell line downregulates constitutively activated phosphatidylinositol 3-kinase/Akt/GSK-3beta signaling and leads to an increased transit time through the G1 phase of the cell cycle.

    Leukemia·2004
    Same author

    Assay for ADP-ribosyl cyclase by reverse-phase high-performance liquid chromatography.

    Analytical biochemistry·2001
    Same author

    Mechanisms involved in alpha6beta1-integrin-mediated Ca(2+) signalling.

    Cellular signalling·2001
    Same author

    Inositol hexakisphosphate increases L-type Ca2+ channel activity by stimulation of adenylyl cyclase.

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2001
    Same journal

    Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

    FEBS letters·2026
    Same journal

    The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

    FEBS letters·2026
    Same journal

    Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

    FEBS letters·2026
    Same journal

    Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

    FEBS letters·2026
    Same journal

    α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.

    FEBS letters·2026
    Same journal

    Modelling stem cell differentiation related processes-A practical overview for biologists.

    FEBS letters·2026
    See all related articles

    Researchers identified a novel calmodulin-binding protein with phosphofructokinase activity. This protein is identical to phosphofructokinase, suggesting calcium-calmodulin regulates enzyme polymerization.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Myosin light chain kinase purification yielded an unexpected calmodulin-binding protein.
    • This protein exhibited phosphofructokinase activity, prompting further investigation.

    Purpose of the Study:

    • To determine the identity of the isolated calmodulin-binding protein.
    • To investigate the relationship between this protein and phosphofructokinase.
    • To explore the regulatory role of calcium-calmodulin on phosphofructokinase.

    Main Methods:

    • Protein purification from crude myosin.
    • Amino acid composition analysis.
    • Antigenic identity testing.
    • Peptide mapping.
    • Calmodulin binding assays.

    Related Experiment Videos

  • Enzyme activity assays.

    • Main Results:

    • Isolation of an 85,000 Mr calmodulin-binding protein.
    • Demonstration of identity to phosphofructokinase via amino acid composition, antigenic properties, and peptide maps.
    • Calmodulin binding capability confirmed for standard phosphofructokinase preparations.
    • Initial findings indicate calcium-calmodulin potent regulation of phosphofructokinase polymerization.

    Conclusions:

    • The isolated calmodulin-binding protein is identical to phosphofructokinase.
    • Phosphofructokinase possesses calmodulin-binding properties.
    • Calcium-calmodulin acts as a potent regulator of phosphofructokinase polymerization, suggesting a novel regulatory mechanism.