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-binding lysozymes.

K Nitta1, H Tsuge, K Shimazaki

  • 1Department of Polymer Science, Faculty of Science, Hokkaido University, Japan.

Biological Chemistry Hoppe-Seyler
|August 1, 1988
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

Anatomy-based surgery to remove thyroglossal duct cyst: two anomalous cases.

The Journal of laryngology and otology·2009
Same author

Glomerular crescents predominantly express cadherin-catenin complex in pauci-immune-type crescentic glomerulonephritis.

Histopathology·2003
Same author

C4d deposition in the glomeruli and peritubular capillaries associated with transplant glomerulopathy.

Clinical transplantation·2003
Same author

Search for nu(e) from the sun at Super-Kamiokande-I.

Physical review letters·2003
Same author

Search for supernova relic neutrinos at Super-Kamiokande.

Physical review letters·2003
Same author

Catheter dysfunction and thrombosis of double-lumen hemodialysis catheters placed in the femoral vein.

Clinical nephrology·2002
Same journal

Cloning and characterization of another lignin peroxidase gene from the white-rot fungus Phanerochaete chrysosporium.

Biological chemistry Hoppe-Seyler·1996
Same journal

Substrate and inhibitor specificity of glutamine cyclotransferase (QC).

Biological chemistry Hoppe-Seyler·1996
Same journal

Reductive activation markedly increases the stability of cathepsins B and L to extracellular ionic conditions.

Biological chemistry Hoppe-Seyler·1996
Same journal

Prognostic value of cathepsins B, H, L, D and their endogenous inhibitors stefins A and B in head and neck carcinoma.

Biological chemistry Hoppe-Seyler·1996
Same journal

Selective inhibition of cyclic AMP-dependent protein kinase by isoquinoline derivatives.

Biological chemistry Hoppe-Seyler·1996
Same journal

Purification of the CIC-0 chloride channel from Torpedo california electroplax identification of a phosphorylation site for cAMP-dependent protein kinase.

Biological chemistry Hoppe-Seyler·1996
See all related articles

Pigeon and equine lysozymes bind calcium ions, with pigeon lysozyme showing stronger binding. This calcium-binding lysozyme gene likely predates avian and mammalian lineage splits, potentially evolving into alpha-lactalbumin.

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Lysozymes are enzymes involved in bacterial cell wall hydrolysis.
  • Calcium ions are known to influence protein structure and function.
  • Previous studies have indicated varied calcium-binding properties among lysozymes.

Purpose of the Study:

  • To investigate and compare the calcium-binding properties of pigeon and equine lysozymes.
  • To determine the evolutionary origins of calcium-binding lysozymes.
  • To explore the potential evolutionary link between calcium-binding lysozyme and alpha-lactalbumin.

Main Methods:

  • Gel filtration chromatography using Bio-Gel P-60.
  • Determination of binding constants through equilibrium dialysis or similar methods.

Related Experiment Videos

  • Amino acid sequence analysis for evolutionary inference.

    • Main Results:

    • Both pigeon and equine lysozymes were found to bind one calcium ion per molecule.
    • The binding constant for pigeon lysozyme (1.6 x 10^7 M^-1) was significantly higher than that for equine lysozyme (2 x 10^6 M^-1) under specified conditions.
    • Phylogenetic analysis suggests the calcium-binding lysozyme gene diverged from its non-calcium-binding counterpart before the split of avian and mammalian lineages.

    Conclusions:

    • Pigeon lysozyme exhibits a higher affinity for calcium ions compared to equine lysozyme.
    • The evolutionary history of calcium-binding lysozyme is ancient, originating before major vertebrate lineage divergences.
    • Calcium-binding lysozyme is a plausible evolutionary precursor to alpha-lactalbumin.