The enzymatic radioiodination of porcine insulin by a system consisting of lactoperoxidase, hydrogen peroxide, and Na125I was compared with a modified chloramine-T technique. Satisfactory specific activity of the labeled hormone was obtained with the enzymatic iodination, with much greater immunoreactivity and stability than after chloramine-T, besides being quite suitable for the measurement o...

Human salivary proteins were enzymically iodinated by the 125I-lactoperoxidase system. The proteins were than subjected to DEAE-cellulose column chromatography, preparative column electrofocusing and thin-layer polyacrylamide-gel electrofocusing. The radioactivity in the resolved protein pools and bands was determined. Results show that salivary proteins differ in their susceptibility to iodina...

Sindbis virus was iodinated by using the enzyme lactoperoxidase, an iodination technique which labels only surface proteins. By this technique, the two viral glycoproteins are labeled, and the internal viral protein is not. The two glycoproteins are iodinated to strikingly different extents. This difference in susceptibility to iodination apparently is due to the position or conformation of the...

In vivo, lactoperoxidase produces hypothiocyanite (OSCN(-)) from thiocyanate (SCN(-)) in the presence of hydrogen peroxide (H2O2); in vitro, iodide (I(-)) can be oxidized into hypoiodite (OI(-)) by this enzyme. The aim of this study was to compare in vitro the anti-Candida effect of iodide versus thiocyanate used as lactoperoxidase substrate to prevent Candida biofilms development. Candida albi...

background: lactoperoxidase (lpo) is one of the most heat-stable enzymes in milk and its inactivation has been proposed for monitoring thermal processes. the aim of this study was to provide information on activity and thermal inactivation behavior of lpo in iranian cow and buffalo milk and whey. methods: sixty cow and buffalo milk samples were collected. the lpo activity was measured using spe...

We have used lactoperoxidase-catalyzed iodination to study the topographical distribution of proteins in free and membrane-bound polysomes and in isolated ribosomal subunits. Free polysomes or rough microsomes were iodinated with 125I and then dissociated into 40 S and 60 S subunits by the use of puromycin/KCl. The separated subunits were iodinated with 13’1 and their protein composition analyz...

Investigation of bovine lacrimal and harderian glands revealed the presence of the enzyme lactoperoxidase, which was isolated and purified. A nonheme, iron-containing protein was identified at the same time. Both proteins are present in milk, mammary glands, and salivary glands. Their roles are discussed: The lactoperoxidase may be important in controlling bacterial flora.