Adsorption of the cationic salivary proteins lactoferrin, lactoperoxidase, lysozyme and histatin 5 to pure (hydrophilic) and methylated (hydrophobized) silica surfaces was investigated by in situ ellipsometry. Effects of concentration (</=10 microgml(-1), for lysozyme </=200 microgml(-1)) and dependence of surface wettability, as well as adsorption kinetics and elutability of adsorbed films by ...

Lactoperoxidase is an enzyme that contributes to the antimicrobial defense in secretory fluids and that has attracted interest as a potential biopreservative for foods and other perishable products. Its antimicrobial activity is based on the formation of hypothiocyanate (OSCN-) from thiocyanate (SCN-), using H2O2 as an oxidant. To gain insight into the antibacterial mode of action of the lactop...

BACKGROUND Saliva contains a number of protective factors such as mucins, immunoglobulins (e.g., IgA, IgG, and IgM), and enzymes (e.g., lysozyme and lactoperoxidases) that play an important role in the maintenance of oral health. The aim of this study was to compare levels of sIgA, histatin-5, and lactoperoxidase in saliva of adolescents with dental caries. MATERIAL AND METHODS Thirty-five ad...

Milk is known to contain proteins (e.g. lactoferrin, lactoperoxidase, immunoglobulins) and free peptides having specific non-nutritional physiological functions. Lactoperoxidase (LP), is undoubtedly important in the case of the human infant, but it potentially has greater significance and functional role in milk industry. LP, a non-haem iron-binding glycoprotein, is a peroxidase enzyme secreted...

Unlike lactoperoxidase and horseradish peroxidase, thyroid peroxidase catalyzed the oxidation of hydroquinone mostly by way of 2-electron transfer. This conclusion could be derived from three independent experiments: ESR measurements of p-benzosemiquinone, trapping the unpaired electron by cytochrome c, and spectrophotometric analysis of catalytic intermediates of the enzymes. The 1-electron fl...

A study of the inhibition of the growth of Streptococcus cremoris 972 by the enzyme lactoperoxidase has shown, in agreement with previous investigations, that the inhibition requires a source of both peroxide and thiocyanate. The thiocyanate may play more than one role. It stabilizes the very dilute solutions of lactoperoxidase employed in these studies, and its oxidation products may be involv...

1. The visible absorption spectrum of peroxidase II, isolated from the uterine tissue of oestradiol-treated rats, and some of its derivatives were recorded. The spectral properties of this enzyme are very similar to eosinophile peroxidase and lactoperoxidase, suggesting that these enzymes may have a similar form of haem as prosthetic group. 2. The uterine peroxidase is modified upon interaction...

Lactoperoxidase, in the presence of hydrogen peroxide and iodide is cytotoxic for human and mouse lymphoid cells, and human erythrocytes. Myeloperoxidase, in amounts equivalent to 1.5 x 10(6) neutrophils, readily replaces lactoperoxidase, and allows the substitution of the iodide ion by chloride. The myeloperoxidase-mediated reaction is rapid, and highly efficient, leading to 85-90% cell death ...