L2005
Lactoperoxidase from bovine milk
lyophilized powder (essentially salt-free), ≥200 units/mg protein
Synonym(s):
Donor:hydrogen peroxide oxidoreductase, Peroxidase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
biological source
bovine milk
form
lyophilized powder (essentially salt-free)
specific activity
≥200 units/mg protein
absorbance ratio
A412/280 nm 0.7-0.9
UniProt accession no.
storage temp.
−20°C
InChI
1S/H2O3/c1-3-2/h1-2H
InChI key
JSPLKZUTYZBBKA-UHFFFAOYSA-N
Gene Information
cow ... LPO(280844)
Looking for similar products? Visit Product Comparison Guide
General description
Lactoperoxidase is a major enzyme present in bovine milk and belongs to the peroxidase family. It is present in both plants and animals. The enzyme structure comprises a single polypeptide chain made up of 612 amino acid residues.
Application
Lactoperoxidase from bovine milk has been used as a standard for milk lactoperoxidase to study the role of H2O2 in the inhibition of Staphylococcus aureus growth by Lactococcus garvieae in the presence of lactoperoxidase in raw milk. It has also been used in lactoperoxidase-mediated iodination to prepare radiolabeled peptides.
Biochem/physiol Actions
Lactoperoxidase contributes to the antimicrobial system of milk by inactivating a wide range of micro-organisms. This lactoperoxidase-mediated antimicrobial system is also identified in human secretions such as tear-fluid, saliva, and milk. Lactoperoxidase catalyzes the oxidation of molecules by releasing H2O2. The product exhibits antimicrobial activity.
Lactoperoxidase catalyzes the oxidation of iodide to iodine by hydrogen peroxide. This activity provides a gentle, specific alternative to chloramine T for the radioiodination of proteins and DNA.
Unit Definition
One unit will oxidize 1.0 μmole of 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) at pH 5.5 at 25 °C.
Analysis Note
Protein determined by Lowry method.
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Céline Delbes-Paus et al.
Food microbiology, 27(7), 924-932 (2010-08-07)
The response of Staphylococcus aureus growth inhibition by Lactococcus garvieae to catalase and milk lactoperoxidase, and its efficiency in raw milk cheese were evaluated. S. aureus and L. garvieae were co-cultivated in broth buffered at pH 6.8, and in raw
Martina Paumann-Page et al.
Redox biology, 46, 102090-102090 (2021-08-27)
Peroxidasin, a heme peroxidase, has been shown to play a role in cancer progression. mRNA expression has been reported to be upregulated in metastatic melanoma cell lines and connected to the invasive phenotype, but little is known about how peroxidasin
Kotaro Sakamoto et al.
Biochemistry and biophysics reports, 12, 135-139 (2017-11-02)
The blood-brain barrier (BBB) is a major obstacle to drug delivery into the central nervous system (CNS), in particular for macromolecules such as peptides and proteins. However, certain macromolecules can reach the CNS via a receptor-mediated transcytosis (RMT) pathway, and
S Linde et al.
International journal of peptide and protein research, 15(5), 495-502 (1980-05-01)
Monoiodoinsulin was prepared using ion exchange chromatography. The isolated monoiodoinsulin showed on polyacrylamide gel electrophoresis two bands with different intensities related to the initial method of iodination. Each of the two bands were isolated from the gel, and determination of
K D Kussendrager et al.
The British journal of nutrition, 84 Suppl 1, S19-S25 (2001-03-10)
Lactoperoxidase (LP) is one of the most prominent enzymes in bovine milk and catalyses the inactivation of a wide range of micro-organisms in the lactoperoxidase system (LP-s). LP-systems are also identified as natural antimicrobial systems in human secretions such as
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service