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1 e) and 42 +/- 9% by dapsone (an inhibitor of lactoperoxidase).
2 cts on colostral IgA, IgM, IgG, lysozyme and lactoperoxidase.
3 5E, E375D, and D225E/E375D mutants of bovine lactoperoxidase.
4 ions catalyzed by horseradish peroxidase and lactoperoxidase.
5 assay product from the reaction catalyzed by lactoperoxidase.
6 d radioiododestannylation in the presence of lactoperoxidase.
7 lycan recognition protein 1, osteopontin and lactoperoxidase.
11 peroxidase (MPO), eosinophil peroxidase, and lactoperoxidase all catalytically consumed NO in the pre
12 conclude that details of the heme pocket of lactoperoxidase allow ligation changes with temperature
13 lutionary lines of the mammalian peroxidases lactoperoxidase and myeloperoxidase revealed the presenc
15 strate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2. via peroxidas
17 he presence of the H2O2-decomposing salivary lactoperoxidase and thiocyanate, which would not otherwi
19 es: microperoxidase, horseradish peroxidase, lactoperoxidase, and hemoglobin, via oxidation of the mo
20 n peroxidases, including myeloperoxidase and lactoperoxidase, bind their prosthetic heme covalently t
21 us quantification of the minor (lactoferrin, lactoperoxidase, bovine serum albumin) and major (a-lact
22 us quantification of the minor (lactoferrin, lactoperoxidase, bovine serum albumin) and major (alpha-
27 nents, including lysozyme, xanthine oxidase, lactoperoxidase, immunoglobulin A, lactoferrin, lipoprot
34 of beta2-microglobulin (beta2m) detected by lactoperoxidase labelling of the high expressor variants
35 glyco(caseino)macropeptide, immunoglobulin, lactoperoxidase, lactoferrin, alpha-lactalbumin and beta
37 ers of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)).
38 n a pH 4 buffer, (2) I(-) in the presence of lactoperoxidase (LPO) and H(2)O(2) in a pH 7 buffer, and
40 ypohalous acid generating peroxidase enzymes lactoperoxidase (LPO) and myeloperoxidase (MPO), nicotin
42 The covalently bound prosthetic group of lactoperoxidase (LPO) has been obtained by hydrolysis of
43 ity of the non-extractable heme of mammalian lactoperoxidase (LPO) has remained unsolved for over 40
49 n peroxidases, including myeloperoxidase and lactoperoxidase (LPO) is the existence of covalent bonds
51 Whether it reacts sufficiently rapidly with lactoperoxidase (LPO) to act as a physiological substrat
52 conformational modification in the adsorbed lactoperoxidase (LPO) which in turns degrades the synthe
53 mide was determined to be a new inhibitor of lactoperoxidase (LPO) with an IC(50) of 0.848.10(-5)M.
55 mer of H2O2 in sheep airway secretions to be lactoperoxidase (LPO), a heme peroxidase previously stud
56 mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thioc
57 dase (MPO), eosinophil peroxidase (EPO), and lactoperoxidase (LPO), homologous members of the mammali
58 adish peroxidase, myeloperoxidase (MPO), and lactoperoxidase (LPO), in the presence of hydrogen perox
60 ic cycle of mammalian peroxidases, including lactoperoxidase (LPO), is binding of hydrogen peroxide t
61 ow show that eosinophil peroxidase (EPO) and lactoperoxidase (LPO), peroxidases known to be enriched
62 prosthetic group from the bovine milk enzyme lactoperoxidase (LPO), termed heme l, is isolated throug
63 ks in partnership with an airway peroxidase, lactoperoxidase (LPO), to produce antimicrobial hypothio
67 doxorubicin (DXR) and daunorubicin (DNR) by lactoperoxidase(LPO)/H(2)O(2) and horseradish peroxidase
68 ve been acquired for resting state mammalian lactoperoxidase, LPO(N), and its six-coordinate, low-spi
69 omponent 3; angiopoietin 2; myeloperoxidase; lactoperoxidase; major histocompatibility complex, class
71 r transcript levels for antioxidant enzymes (lactoperoxidase, microsomal glutathione S-transferase 2
73 suggest that heme-protein ester linkages in lactoperoxidase occur between the two hydroxyl groups of
74 2) were activated by horseradish peroxidase, lactoperoxidase, or cytochrome P450, 87-440 micromol of
76 trong induction of oxidase genes, e.g., Lpo (lactoperoxidase), p22-phox, p47-phox, and Gp91, in NHK/B
77 nate to these samples (0.4 mM; substrate for lactoperoxidase) restored their ability to scavenge H2O2
80 rric rhombic heme spectrum became similar to lactoperoxidase, the standard reduction potential of the
81 s needed only in certain situations, whereas lactoperoxidase, useful at all times, does not change it
82 C, but at higher temperatures a decrement of lactoperoxidase, vitamin B6 and folic acid was observed.
84 bserved when human myeloperoxidase or bovine lactoperoxidase was substituted for horseradish peroxida
85 utaredoxin, albumin, beta-lactoglobulin, and lactoperoxidase were identified in the selenium-containi
86 e serum albumin, bovine catalase, and bovine lactoperoxidase were used to carry out peptide mass fing