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

Lactoperoxidase from human colostrum.

B Langbakk1, T Flatmark

  • 1Department of Biochemistry, University of Bergen, Norway.

The Biochemical Journal
|May 1, 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

The progenitor cell marker NG2/MPG promotes chemoresistance by activation of integrin-dependent PI3K/Akt signaling.

Oncogene·2008
Same author

An experimental large animal model for the assessment of bioartificial liver support systems in fulminant hepatic failure.

Scandinavian journal of gastroenterology·2002
Same author

High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.

Journal of molecular biology·2001
Same author

Transient up-regulation of liver mitochondrial thymidine kinase activity in proliferating mitochondria.

IUBMB life·2001
Same author

Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation.

Analytical biochemistry·2001
Same author

Conjugation of phenylalanine hydroxylase with polyubiquitin chains catalysed by rat liver enzymes.

Biochimica et biophysica acta·2001
Same journal

Reshaping the glycocalyx: the SULF extracellular endosulfatases as molecular editors of heparan Sulfate.

The Biochemical journal·2026
Same journal

Mechanistic insights into acetylated histone recognition by the CECR2 bromodomain.

The Biochemical journal·2026
Same journal

Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

The Biochemical journal·2026
Same journal

Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

The Biochemical journal·2026
Same journal

Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

The Biochemical journal·2026
Same journal

Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

The Biochemical journal·2026
See all related articles

Human colostrum contains lactoperoxidase, an enzyme crucial for immune defense. This study details its purification and characterization, revealing properties similar to the bovine enzyme.

Area of Science:

  • Biochemistry
  • Enzymology
  • Human Physiology

Background:

  • Human colostrum is a vital source of bioactive compounds.
  • Lactoperoxidase (EC 1.11.1.7) plays a significant role in innate immunity.
  • Previous studies have characterized bovine lactoperoxidase.

Purpose of the Study:

  • To confirm and characterize lactoperoxidase in human colostrum.
  • To develop purification methods for human lactoperoxidase.
  • To compare human lactoperoxidase properties with its bovine counterpart.

Main Methods:

  • Multistep protein purification procedures.
  • Immunoaffinity chromatography using an antibody against bovine lactoperoxidase B.
  • Concanavalin A-Sepharose chromatography.

Related Experiment Videos

  • Spectroscopic analysis (Soret peak).

    • Main Results:

    • Human colostrum contains lactoperoxidase, comprising approximately 0.004% of total protein.
    • A 32-fold purification was achieved via a modified multistep procedure.
    • Immunoaffinity chromatography yielded a 1450-fold purification in a single step.
    • The enzyme is a glycoprotein with spectral and molecular weight (Mr 80,000) similar to bovine lactoperoxidase.

    Conclusions:

    • Human colostrum is a source of lactoperoxidase.
    • Immunoaffinity chromatography is highly effective for purifying human lactoperoxidase.
    • Human lactoperoxidase shares characteristics with bovine lactoperoxidase, suggesting conserved functional properties.