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

Calcium-dependent binding between calmodulin and lysozyme.

J F Fierro1, M A Pajares, C Hardisson

  • 1Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.

FEBS Letters
|April 10, 1989
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

Guidelines for enhanced recovery after cardiac surgery. Consensus document of Spanish Societies of Anesthesia (SEDAR), Cardiovascular Surgery (SECCE) and Perfusionists (AEP).

Revista espanola de anestesiologia y reanimacion·2021
Same author

Human lactoferrin triggers a mitochondrial- and caspase-dependent regulated cell death in Saccharomyces cerevisiae.

Apoptosis : an international journal on programmed cell death·2015
Same author

Structure-function relationships in methionine adenosyltransferases.

Cellular and molecular life sciences : CMLS·2008
Same author

Early effects of copper accumulation on methionine metabolism.

Cellular and molecular life sciences : CMLS·2008
Same author

Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism?

Cellular and molecular life sciences : CMLS·2006
Same author

Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane.

Biochemistry. Biokhimiia·2003
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
Same journal

Overlapping gut microbiome signatures in aging and disease are characterized by enrichment of medication-associated oral microbes in the gut.

FEBS letters·2026
Same journal

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3.

FEBS letters·2026
Same journal

Mixed-class J-domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly.

FEBS letters·2026
See all related articles

Calcium-dependent calmodulin binds to hen egg-white lysozyme. This interaction was confirmed using biochemical methods, but lysozyme

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Calmodulin is a key calcium-binding protein regulating eukaryotic cellular processes.
  • Lysozyme, found in hen egg-white, possesses antimicrobial properties.

Purpose of the Study:

  • To investigate the potential interaction between calmodulin and hen egg-white lysozyme.
  • To determine if calcium-dependent calmodulin affects lysozyme's antimicrobial activity.

Main Methods:

  • Utilized electroblotting with biotinylated calmodulin and avidin-alkaline phosphatase detection.
  • Employed affinity chromatography on a calmodulin-coated gel column.
  • Assessed antimicrobial activity of lysozyme in the presence of Ca2+-calmodulin.

Main Results:

Related Experiment Videos

  • Calmodulin binding to hen egg-white lysozyme was confirmed in a calcium-dependent manner.
  • The antimicrobial efficacy of lysozyme remained unchanged when bound to Ca2+-calmodulin.

Conclusions:

  • Calmodulin can bind to hen egg-white lysozyme in a calcium-dependent fashion.
  • The interaction between calmodulin and lysozyme does not alter the lysozyme's inherent antimicrobial function.