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

Calmodulin-binding peptides isolated from alpha-casein peptone

K Kizawa1, K Naganuma, U Murakami

  • 1Biochemistry Laboratory, Kanebo Ltd, Odawara, Japan.

The Journal of Dairy Research
|November 1, 1995
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

Effects of combined GABA and L-theanine supplementation on sleep quality: an exploratory study.

European review for medical and pharmacological sciences·2026
Same author

Expression and translocation of aquaporin-2 in the endolymphatic sac in patients with Meniere's disease.

Journal of neuroendocrinology·2010
Same author

Behavioral assessment and identification of a molecular marker in a salicylate-induced tinnitus in rats.

Neuroscience·2009
Same author

Compact diode-pumped all-solid-state femtosecond Cr(4+):YAG laser.

Optics letters·2009
Same author

Optical parametric oscillator incoherent spectroscopy.

Optics letters·2009
Same author

Characteristics of femtosecond pulses near 1.5 microm in a self-mode-locked Cr(4+):YAG laser.

Optics letters·2009

Researchers identified specific alpha-casein peptides that effectively inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase. These peptides show strong binding affinities to calmodulin, similar to natural signaling molecules.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Calmodulin is a crucial calcium-binding protein involved in numerous cellular signaling pathways.
  • Cyclic nucleotide phosphodiesterases (PDEs) are enzymes that regulate intracellular levels of cyclic nucleotides, impacting various physiological processes.
  • Alpha-casein, a major milk protein, is a source of bioactive peptides with diverse biological functions.

Purpose of the Study:

  • To isolate and characterize peptides from alpha-casein that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase.
  • To determine the specific sequences of these inhibitory peptides.
  • To compare the calmodulin-binding affinities of these peptides with known endogenous ligands.

Main Methods:

  • Pepsin digestion of alpha-casein to generate peptide fragments.

Related Experiment Videos

  • Isolation and purification of specific peptides from the digest.
  • Biochemical assays to measure inhibition of calmodulin-dependent cyclic nucleotide phosphodiesterase activity.
  • Amino acid sequencing to identify the isolated peptides.

    • Main Results:

    • Identified three peptides from alpha-casein (sequences 164-179, 183-206, and 183-207) that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase.
    • These peptides demonstrated significant inhibitory activity in the micromolar range (1-50 microM).
    • The peptides selectively inhibited calmodulin-induced enzyme activity, leaving basal activity unaffected.
    • The binding affinities of these alpha-casein-derived peptides for calmodulin were found to be comparable to those of endogenous neurohormones and other calmodulin-binding proteins.

    Conclusions:

    • Alpha-casein is a source of novel peptides with potent calmodulin-binding and inhibitory properties.
    • These peptides represent potential modulators of calmodulin-mediated signaling pathways.
    • The findings suggest a role for dietary peptides in regulating cellular signaling processes involving calmodulin.