gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.


lactoperoxidase, salivary peroxidase
This gene encodes an oxidoreductase secreted from salivary, mammary, and other mucosal glands that functions as a natural antibacterial agent. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, myeloperoxidase, HAD, Lactoferrin
Papers on lactoperoxidase
Enzymatic oxidative biodegradation of nanoparticles: Mechanisms, significance and applications.
Kagan et al., Pittsburgh, United States. In Toxicol Appl Pharmacol, Feb 2016
Here, we review the role and contribution of different oxidative enzymes of inflammatory cells - myeloperoxidase, eosinophil peroxidase, lactoperoxidase, hemoglobin, and xanthine oxidase - to the reactions of nanoparticle biodegradation.
Hypothiocyanite produced by human and rat respiratory epithelial cells inactivates extracellular H1N2 influenza A virus.
Rada et al., Athens, United States. In Inflamm Res, Jan 2016
TREATMENT: A/swine/Illinois/02860/09 (swH1N2) influenza A virions were added to the apical side of airway cells for 1 h in the presence or absence of lactoperoxidase or thiocyanate.
Formation of cyanogen iodide by lactoperoxidase.
Arnhold et al., Leipzig, Germany. In J Inorg Biochem, Jan 2016
The haem protein lactoperoxidase (LPO) is an important component of the anti-microbial immune defence in external secretions and is also applied as preservative in food, oral care and cosmetic products.
Preparation of lactoperoxidase incorporated hybrid nanoflower and its excellent activity and stability.
Özdemir et al., Kayseri, Turkey. In Int J Biol Macromol, Jan 2016
UNASSIGNED: We report a green approach to synthesize lactoperoxidase (LPO) enzyme and metal ions hybrid nanoflowers (HNFs) and investigate mechanism underlying formation and enhanced catalytic activity and stability under different experimental parameters.
The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII.
Alwasel et al., Erzurum, Turkey. In J Enzyme Inhib Med Chem, Nov 2015
Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and eukaryotic organisms and involved in cellular detoxification mechanisms.
Biochemical mechanisms and therapeutic potential of pseudohalide thiocyanate in human health.
Day et al., Denver, United States. In Free Radic Res, Jun 2015
This reaction is catalyzed by chordate peroxidases (e.g., myeloperoxidase and lactoperoxidase), occurring in human secretory mucosa, including the oral cavity, airway, and alimentary tract, and regulates resident and transient flora as part of innate immunity.
Protection of lactoperoxidase activity with sugars during lyophilization and evaluation of its antibacterial properties.
Najafi et al., Eşfahān, Iran. In Res Pharm Sci, Mar 2015
The purpose of the present study was to compare the stabilizing effect of four disaccharides alone or in combination on the lactoperoxidase (LP) derived from bovine milk during lyophilization.
Molecular mechanisms of taste recognition: considerations about the role of saliva.
Fábián et al., Denmark. In Int J Mol Sci, 2014
Other proteins like glucagon-like peptide-1, salivary immunoglobulin-A, zinc-α-2-glycoprotein, salivary lactoperoxidase, salivary prolactin-inducible protein and salivary molecular chaperone HSP70/HSPAs were also expected to play an important role.
Disorder in milk proteins: structure, functional disorder, and biocidal potentials of lactoperoxidase.
Redwan et al., Jiddah, Saudi Arabia. In Curr Protein Pept Sci, 2014
Lactoferrin and lactoperoxidase (LPO) are known to possess prominent biocidal activity, serving as efficient antibiotics and antiviral agents against a wide spectrum of bacteria, fungi, and viruses.
Mode of action of lactoperoxidase as related to its antimicrobial activity: a review.
Jijakli et al., Gembloux, Belgium. In Enzyme Res, 2013
Lactoperoxidase is a member of the family of the mammalian heme peroxidases which have a broad spectrum of activity.
Expression of lactoperoxidase in differentiated mouse colon epithelial cells.
Chu et al., Duarte, United States. In Free Radic Biol Med, 2012
methylation of the Lpo intragenic CpG island was not directly induced by inflammation, because dextran sulfate sodium-induced colitis did not increase DNA methylation in B6 DKO colon. Also, Lpo DNA methylation is not correlated with gene expression
Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases.
Abu-Soud et al., Detroit, United States. In Plos One, 2010
LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function.
First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases.
Singh et al., New Delhi, India. In J Biol Inorg Chem, 2010
Results describe the crystal structure of the complex of lactoperoxidase and 3-amino-1,2,4-triazole (amitrole), which revealed the presence of two ligand molecules, one in the substrate binding site and the second in the hydrophobic channel.
Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases: binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7 A resolution.
Singh et al., New Delhi, India. In J Biol Chem, 2010
LPO can be used for INH activation. It also indicates that the conversion of INH into isonicotinoyl radical by LPO may be the cause of INH toxicity.
Binding modes of aromatic ligands to mammalian heme peroxidases with associated functional implications: crystal structures of lactoperoxidase complexes with acetylsalicylic acid, salicylhydroxamic acid, and benzylhydroxamic acid.
Singh et al., New Delhi, India. In J Biol Chem, 2009
The structures of three complexes of LPO with aromatic substrate, acetylsalicylic acid, and two aromatic inhibitors salicylhydroxamic acid and benzylhydroxamic acid indicate the distinctiveness in their modes of binding as a substrate and as an inhibitor.
Catalytic sites of hemoprotein peroxidases.
Ortiz de Montellano, San Francisco, United States. In Annu Rev Pharmacol Toxicol, 1991
This inference is supported by experimental results on the Coprinus macrorhizus peroxidase (52), manganese peroxidase (51), lignin peroxidase (50) and, less definitively, lactoperoxidase (90).
Breast milk and infection.
Jelliffe et al., In Lancet, 1981
Of the antiinfective substances in human milk, lysozyme was omitted, as were the bifidus factor, the antistaphylococcus factor, antitoxins for neutralizing Vibrio cholerae and Escherichia coli, lactoperoxidase, and volatile fatty acids.
Isolation of a biologically active macrophage receptor for the third component of complement.
Atkinson et al., In Nature, 1981
It is a cell-surface macromolecule (labelled with 125I and lactoperoxidase) which, in its isolated state, retains the ability to bind both C3 and C3b.
Peroxidase-mediated virucidal systems.
Ray et al., In Science, 1970
Peroxidase (myeloperoxidase or lactoperoxidase), hydrogen peroxide, and a halide such as iodide, bromide, or chloride form a potent virucidal system that is effective against polio and vaccinia viruis, particularly at a low pH.
Lactoperoxidase: identification and isolation from Harderian and lacrimal glands.
Allen et al., In Science, 1966
Investigation of bovine lacrimal and harderian glands revealed the presence of the enzyme lactoperoxidase, which was isolated and purified.
share on facebooktweetadd +1mail to friends