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Results for “Iodide Peroxidase”

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At least 19 recordsLinked to original sources
PubMed1978

The characterization of n-butanol-pseudosolubilized and trypsin-solubilized porcine thyroid iodide peroxidase.

Porcine thyroid peroxidase (Iodide: hydrogen-peroxide oxidoreductase, EC 1.11.1.8) was solubilized by proteolytic and non-proteolytic procedures. A kinetic and physical study was undertaken to ascertain the catalytic properties of the peroxidase prepared by the two purported solubilization procedures. Where possible, the properties of the two enzyme preparations were compared with the original microsomal preparation. The n-butanol-solubilized thyroid iodide peroxidase is not truly soluble, but exists as a large molecular weight lipoprotein aggregate. The trypsin-solubilized thyroid iodide peroxidase is truly soluble, active, and contains lipids. The microsomes, butanol-pseudosolubilized enzyme, and trypsin-solubilized enzyme have similar kinetic properties such as pH optima, Km for iodide and H2O2, sigmoid character of the saturation curves, substrate inhibition, and inhibition by 3,5-diiodotyrosine. Since the proteolytic solubilization procedure produced a soluble peroxidase with catalytic properties similar to the microsomal preparation, trypsin-solubilized peroxidase can be studied with reasonable assurance that its properties are essentially unaltered and are not artifacts of the solubilization procedure.

Animals↗
PubMed1980

Binding of iproniazid to the polymeric forms of iodide peroxidase.

14C labelled iproniazid binds to iodide peroxidase more effectively in low ionic strength buffer than in high ionic strength buffer, suggesting preferential binding to the monomeric form of iodide peroxidase. During column chromatography, under conditions that separate iodide peroxidase into multiple forms, iproniazid is bound selectively to the monomeric form. Thus, this antithyroid agent appears to bind preferentially to the monomeric enzyme form, or possibly to cause dissociation of the polymeric to the monomeric form.

Animals↗
PubMed1975

Studies on human iodide peroxidase: its activity in various thyroid disorders.

Iodide peroxidase activities in the human thyroid gland were measured in various thyroid disorders. The peroxidase activities in the thyroid gland revealed high values in Graves' disease, normal levels in thyroid adenoma and low values in thyroid carcinoma as compared to those in normal thyroid glands. A high activity of this enzyme was observed in toxic adenoma. The same results were observed whether 10% (W/V) homogenate or mitochondrial and microsomal fractions of the thyroid gland were used.

Adenoma↗
PubMed1990

Histochemical determination of iodide peroxidase activity in various thyroid disorders.

We developed a histochemical method to demonstrate iodide peroxidase activity in various thyroid disorders and compared it with the biochemical and ultrastructural-cytochemical methods. All of the 26 adenomatous goiters and 43 follicular adenomas were peroxidase-positive. In the 74 cases of thyroid carcinomas examined, about half of the follicular carcinomas (17 of 33 patients), and a few papillary carcinomas (3 of 41 patients) were peroxidase-positive. Peroxidase-negative cases were seen in 70% (52 of 74 patients) of the follicular and papillary carcinomas. All the non-tumorous thyroid tissues adjacent to various disorders were peroxidase-positive. Since our histochemically demonstrated peroxidase activities almost parallel those determined biochemically and ultrastructural-cytochemically, we conclude that histochemical examination is a simple and useful method for the detection of peroxidase activity. As for the relationships between histochemically proved peroxidase activity and the histology of tumors, the histological differentiation of tumors was not consistent with their functional differentiation classified according to peroxidase activity.

Adenocarcinoma↗
PubMed2003

Susceptibility of Fusobacterium nucleatum to killing by peroxidase-iodide-hydrogen peroxide combination in buffer solution and in human whole saliva.

Some Gram-negative anaerobic bacteria have been associated with the infection of tooth supporting tissues, i.e. periodontitis. Of these bacteria, Fusobacterium nucleatum is sensitive to lactoperoxidase/myeloperoxidase-iodide-hydrogen peroxide system in vitro, but salivary concentrations of thiocyanate abolishes the bactericidality. These bacteria are located in periodontal pockets, on oral mucosa and in saliva. Although F. nucleatum most probably does not belong to the group of main periodontal pathogens, it sustains its proportion in the periodontal flora when gingivitis progresses to periodontitis. In this study, the sensitivity of F. nucleatum to different horseradish peroxidase-iodide-hydrogen peroxide combinations was tested both in buffer and in sterilized human whole saliva. Horseradish peroxidase was chosen because it does not bind thiocyanate at pH > or = 6. After 1h incubation at 37 degrees C, the cell viability was estimated by plate count and with flow cytometer using LIVE/DEAD BacLight kit (Molecular Probes, USA). In saliva, the horseradish peroxidase (50 microg/mL)-iodide (2.5 mM)-hydrogen peroxide (2.5 mM) combination decreased the amount of viable bacteria to 37% compared to 85% in the control without any of the components when measured with flow cytometer. Replacement of buffer by saliva decreased the bactericidality of the peroxidase system. However, in buffer less iodide and hydrogen peroxide was needed to produce significant decrease in the number of viable bacteria when measured by plate count than with flow cytometer. Our study shows that horseradish peroxidase-iodide-hydrogen peroxide combination is able to kill F. nucleatum cells in saliva. Horseradish peroxidase-iodide-hydrogen peroxide combination may be useful to diminish the degree of re-colonization of periodontitis-associated bacteria after periodontal therapy and to inhibit the transmission of these bacteria via saliva.

Journal Article↗
PubMed2003

Determination of safety levels of horseradish peroxidase-iodide system to human gingival keratinocytes and fibroblasts in vitro.

The peroxidase-iodide (I-) system is a potential antimicrobial agent, and its bacteriocidal activity against various periodontal bacteria has been shown in many studies. The aim of this study was to investigate the possible cytotoxic effects of a non-physiological horseradish peroxidase (HRP)-I- system on human gingival keratinocytes and fibroblasts. Immortalized human skin keratinocyte cell line was used as a reference. Three indicators were studied: membrane permeability (trypan blue staining), cell growth (crystal violet staining) and metabolic activity (alamarBlue stain). The cells were cultured in microtitration plates, and the most commonly used exposure time to the HRP system was 1 h. The effects of HRP system on cell growth and metabolic activity were observed at lower I- and H2O2 concentrations than its effects on membrane permeability. Gingival fibroblasts were more prone to detachment than keratinocyte cell lines, but no differences in changes of growth or metabolic activities were observed between gingival fibroblasts and gingival keratinocytes. The highest concentrations of the HRP-I- system components which did not have any significant detrimental effects on the metabolic activity and cell growth of gingival keratinocytes and fibroblasts were: 50 microg/ml HRP, 500 micromol/L I- and 500 micromol/L H2O2. Although this system has been shown to be antibacterial against oral bacteria, no recommendations about the usage of the HRP-I- system in oral cavity can be made yet due to the in vitro nature of this study. Our results form the basis for future safety studies investigating the chronic toxicity of this system to oral epithelium.

Cell Division↗
PubMed1988

Target and nontarget actions of phenthoate and carbofuran: brain acetylcholinesterase, kidney iodide peroxidase, and blood thyroxine profiles in Channa punctatus.

Phenthoate- and carbofuran-containing insecticides are widely used by Indian farmers, thus endangering fish by exposing them to the hazards of a chronic low dose of these xenobiotics. Channa punctatus, cultivated under paddy-cum-fish culture programs, was treated with 176 ppb phenthoate, 333 ppb carbofuran, or a mixture of 88 ppb phenthoate plus 250 ppb carbofuran for 15 days. The rate of mortality was 10% in all treatments. These xenobiotics caused significant inhibition of brain acetylcholinesterase concomitant with low kidney iodide peroxidase activity and depressed blood thyroxine levels. It is surmised that phenthoate and carbofuran compounds are capable of significantly influencing the hormonal status of fish which is mediated via their target action on the nervous system.

Acetylcholinesterase↗