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L2005

Sigma-Aldrich

Lactoperoxidase from bovine milk

lyophilized powder (essentially salt-free), ≥200 units/mg protein

Synonyme(s) :

Donor:hydrogen peroxide oxidoreductase, Peroxidase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine milk

Forme

lyophilized powder (essentially salt-free)

Activité spécifique

≥200 units/mg protein

Rapport des absorbances

A412/280 nm 0.7-0.9

Numéro d'accès UniProt

Température de stockage

−20°C

InChI

1S/H2O3/c1-3-2/h1-2H

Clé InChI

JSPLKZUTYZBBKA-UHFFFAOYSA-N

Informations sur le gène

cow ... LPO(280844)

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Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

One unit will oxidize 1.0 μmole of 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) at pH 5.5 at 25 °C.

Remarque sur l'analyse

Protein determined by Lowry method.

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
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

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