ライフサイエンスコーパス: lactoperoxidase

1 e) and 42 +/- 9% by dapsone (an inhibitor of lactoperoxidase).

2 5E, E375D, and D225E/E375D mutants of bovine lactoperoxidase.

3 ions catalyzed by horseradish peroxidase and lactoperoxidase.

4 assay product from the reaction catalyzed by lactoperoxidase.

5 d radioiododestannylation in the presence of lactoperoxidase.

6 cts on colostral IgA, IgM, IgG, lysozyme and lactoperoxidase.

7 Bovine lactoperoxidase activity was hindered by viscosity chang

8 Lactoperoxidase activity was not detected.

9 peroxidase (MPO), eosinophil peroxidase, and lactoperoxidase all catalytically consumed NO in the pre

10 conclude that details of the heme pocket of lactoperoxidase allow ligation changes with temperature

11 lutionary lines of the mammalian peroxidases lactoperoxidase and myeloperoxidase revealed the presenc

12 strate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2. via peroxidas

13 presence of airway surface liquid components lactoperoxidase and thiocyanate (SCN(-)).

14 he presence of the H2O2-decomposing salivary lactoperoxidase and thiocyanate, which would not otherwi

15 es: microperoxidase, horseradish peroxidase, lactoperoxidase, and hemoglobin, via oxidation of the mo

16 n peroxidases, including myeloperoxidase and lactoperoxidase, bind their prosthetic heme covalently t

17 We also show that lactoperoxidase can oxidize pyocyanin, thereby diminishi

18 Method I is lactoperoxidase-catalyzed oxidation of SCN(-) by H(2)O(2

19 The dual oxidase-thiocyanate-lactoperoxidase (Duox/SCN(-)/LPO) system generates the m

20 In contrast to lactoperoxidase, horseradish peroxidase remains high-spi

21 de-out vesicles were [125I]radioiodinated by lactoperoxidase in the same vessel.

22 Optical spectra of lactoperoxidase indicate that the iron changes from high

23 The heme in lactoperoxidase is attached to the protein by ester bond

24 The active site of lactoperoxidase is not as tightly constrained at low pH

25 The iron of lactoperoxidase is predominantly high-spin at ambient te

26 of beta2-microglobulin (beta2m) detected by lactoperoxidase labelling of the high expressor variants

27 glyco(caseino)macropeptide, immunoglobulin, lactoperoxidase, lactoferrin, alpha-lactalbumin and beta

28 ers of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)).

29 Bovine lactoperoxidase (LPO) and lactoferrin (LF) are suitable

30 ypohalous acid generating peroxidase enzymes lactoperoxidase (LPO) and myeloperoxidase (MPO), nicotin

31 The covalently bound prosthetic group of lactoperoxidase (LPO) has been obtained by hydrolysis of

32 ity of the non-extractable heme of mammalian lactoperoxidase (LPO) has remained unsolved for over 40

33 First, lactoperoxidase (LPO) in the airways catalyzes oxidation

34 The reactions of lactoperoxidase (LPO) intermediates compound I, compound

35 Heme reduction of ferric lactoperoxidase (LPO) into its ferrous form initially le

36 Lactoperoxidase (LPO) is an enzyme with antimicrobial pr

37 n peroxidases, including myeloperoxidase and lactoperoxidase (LPO) is the existence of covalent bonds

38 Lactoperoxidase (LPO) reacts with H(2)O(2) to sequential

39 Whether it reacts sufficiently rapidly with lactoperoxidase (LPO) to act as a physiological substrat

40 mide was determined to be a new inhibitor of lactoperoxidase (LPO) with an IC(50) of 0.848.10(-5)M.

41 The H(2)O(2)-dependent reaction of lactoperoxidase (LPO) with sperm whale myoglobin (SwMb)

42 mer of H2O2 in sheep airway secretions to be lactoperoxidase (LPO), a heme peroxidase previously stud

43 mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thioc

44 dase (MPO), eosinophil peroxidase (EPO), and lactoperoxidase (LPO), homologous members of the mammali

45 adish peroxidase, myeloperoxidase (MPO), and lactoperoxidase (LPO), in the presence of hydrogen perox

46 This reaction is not observed with lactoperoxidase (LPO), in which the heme is covalently b

47 ic cycle of mammalian peroxidases, including lactoperoxidase (LPO), is binding of hydrogen peroxide t

48 ow show that eosinophil peroxidase (EPO) and lactoperoxidase (LPO), peroxidases known to be enriched

49 prosthetic group from the bovine milk enzyme lactoperoxidase (LPO), termed heme l, is isolated throug

50 Human airway mucosa synthesizes and secretes lactoperoxidase (LPO).

51 o investigate protein radical formation from lactoperoxidase (LPO).

52 doxorubicin (DXR) and daunorubicin (DNR) by lactoperoxidase(LPO)/H(2)O(2) and horseradish peroxidase

53 ve been acquired for resting state mammalian lactoperoxidase, LPO(N), and its six-coordinate, low-spi

54 PT was radioiodinated by the lactoperoxidase method which preferentially radioiodinat

55 r transcript levels for antioxidant enzymes (lactoperoxidase, microsomal glutathione S-transferase 2

56 In addition to HRP, lactoperoxidase, myeloperoxidase, and HL-60 cells, natur

57 suggest that heme-protein ester linkages in lactoperoxidase occur between the two hydroxyl groups of

58 2) were activated by horseradish peroxidase, lactoperoxidase, or cytochrome P450, 87-440 micromol of

59 cose, peroxynitrite, horseradish peroxidase, lactoperoxidase, or lipoxygenase.

60 trong induction of oxidase genes, e.g., Lpo (lactoperoxidase), p22-phox, p47-phox, and Gp91, in NHK/B

61 nate to these samples (0.4 mM; substrate for lactoperoxidase) restored their ability to scavenge H2O2

62 At low pH, lactoperoxidase shows a solvent-dependent transition; th

63 however, that H2O2 is mainly consumed by the lactoperoxidase system.

64 rric rhombic heme spectrum became similar to lactoperoxidase, the standard reduction potential of the

65 s needed only in certain situations, whereas lactoperoxidase, useful at all times, does not change it

66 Lactoperoxidase was purified 409-fold from the synthesiz

67 bserved when human myeloperoxidase or bovine lactoperoxidase was substituted for horseradish peroxida

68 utaredoxin, albumin, beta-lactoglobulin, and lactoperoxidase were identified in the selenium-containi

69 e serum albumin, bovine catalase, and bovine lactoperoxidase were used to carry out peptide mass fing

70 We have studied lactoperoxidase, which prevents bacterial colonization o