Bovine lactoperoxidase (LPO) ELISA kit

1. 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. PMID: 28594102
2. establish urate as a likely physiological substrate for LPO that will influence host defense and give rise to reactive electrophilic metabolites PMID: 24928513
3. 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. PMID: 22886082
4. LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function. PMID: 22132121
5. 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. PMID: 20461536
6. 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. PMID: 19907057
7. at higher temperature, the protein hydrophobic core, rich in alpha-helices, unfolds with concomitant disruption of the catalytic heme pocket & activity loss. the stabilizing role of the disulfide bridges and the covalently bound heme cofactor are shown. PMID: 17698426
8. Comparative spectroscopic analysis of the ferrous forms of LPO, wild-type MPO and the variants demonstrate that a single, stable ferrous form of MPO is present only in those proteins which retain an intact sulfonium linkage. PMID: 18359301
9. lactoperoxidase containing thiocyanate (SCN(-)) 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 PMID: 19167310
10. The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. PMID: 19339248
11. 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. PMID: 19465478

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KEGG: bta:280844

STRING: 9913.ENSBTAP00000016986

UniGene: Bt.4784