L2005
Lactoperoxidase from bovine milk
lyophilized powder (essentially salt-free), ≥200 units/mg protein
Synonym(s):
Donor:hydrogen peroxide oxidoreductase, Peroxidase
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£43.30
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£118.00
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£244.00
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£416.00
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Estimated to ship on02 December 2025Details
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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
SMILES string
[O+H2]O[O-]
InChI
1S/H2O3/c1-3-2/h1-2H
InChI key
JSPLKZUTYZBBKA-UHFFFAOYSA-N
Gene Information
cow ... LPO(280844)
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1 of 4
This Item | 61328 | 77332 | M6908 |
|---|---|---|---|
| specific activity ≥200 units/mg protein | specific activity ≥150 U/mg | specific activity ~150 U/mg | specific activity ≥50 units/mg protein |
| Gene Information cow ... LPO(280844) | Gene Information cow ... LPO(280844) | Gene Information - | Gene Information human ... MPO(4353) |
| biological source bovine milk | biological source - | biological source horseradish | biological source human leucocytes |
| form lyophilized powder (essentially salt-free) | form powder | form powder | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| UniProt accession no. | UniProt accession no. | UniProt accession no. - | UniProt accession no. |
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.[1]
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.[2] It has also been used in lactoperoxidase-mediated iodination to prepare radiolabeled peptides.[3]
Biochem/physiol Actions
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.
Lactoperoxidase contributes to the antimicrobial system of milk[2] 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.[1]
Analysis Note
Protein determined by Lowry method.
Other Notes
One unit will oxidize 1.0 μmole of 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) at pH 5.5 at 25 °C.
used together
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
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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
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
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
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
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
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