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LPO encodes an oxidoreductase secreted from salivary, mammary, and other mucosal glands that functions as a natural antibacterial agent.
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Bovine LPO enzyme was effectively inhibited by phenolic molecules. Ki values of these natural products were found as 0.20 +/- 0.09, 0.22 +/- 0.17, 0.49 +/- 0.11, 0.49 +/- 0.27, and 1.20 +/- 0.25 muM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.
establish urate as a likely physiological substrate for LPO that will influence host defense and give rise to reactive electrophilic metabolites
Studied the 3-dimensional structure of CO-LPO at 2.0A resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm(-1) resolution.
LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function.
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.
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.
Comparative spectroscopic analysis of the ferrous forms of LPO, wild-type MPO (show MPO Proteins) and the variants demonstrate that a single, stable ferrous form of MPO (show MPO Proteins) is present only in those proteins which retain an intact sulfonium linkage.
lactoperoxidase containing thiocyanate (SCN (show SRI Proteins)(-)) and hypothiocyanate (OSCN(-)) ions were purified and crystallized; the structure was determined at 2.3-A resolution and refined to R(cryst) and R(free) factors of 0.184 and 0.221, respectively
The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN (show SRI Proteins)(-)) has been determined at 2.4A resolution.
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.
The crystal structure of the complex of LPO with MZY showed that MZY bound to LPO in the substrate-binding site on the distal heme side. MZY was oriented in the substrate-binding site in such a way that the sulfur atom is at a distance of 2.58 A from the heme iron
LPO mRNA was undetectable in the gastric mucosa.
High intensity of caries is associated with increased levels of some salivary components - sIgA, histatin-5 (show HTN3 Proteins) and lactoperoxidase.
a functional LPO system exists in human airways and may contribute to airway host defense against infection
lactoperoxidase may play an important role in the metabolic events associated with Parkinson's disease
Analysis of the role of thiocyanate (SCN (show SRI Proteins)-), in modulating the catalytic activity of myeloperoxidase (MPO (show MPO Proteins)) and other members of the lactoperoxidase (LPO) and eosinophil peroxidase (EPO (show EPX Proteins))
Splice variants may contribute to LPO molecular heterogeneity and its regulation by intracellular compartmental localization in respiratory epithelium.
we postulate that Lpo upregulation in the intestinal epithelium of miR (show MLXIP Proteins)-10a deficient mice together with the predominant abundance of estrogens in female animals mainly accounts for the sex-related cancer phenotype we observed
methylation of the Lpo intragenic CpG island was not directly induced by inflammation, because dextran sulfate sodium-induced colitis did not increase DNA methylation (show HELLS Proteins) in B6 DKO colon. Also, Lpo DNA methylation (show HELLS Proteins) is not correlated with gene expression
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.
, salivary peroxidase
, airway lactoperoxidase