Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We analyzed the radiation-induced changes in the flow rate and protein composition of stimulated whole saliva in eleven patients treated for malignant conditions of the head and neck. In all patients the radiation field covered all major salivary glands and a large area of the oral mucosa. Paraffin-stimulated whole saliva samples were collected once 2 to 21 days before therapy and then after 20, 40, and 60 gray (Gy) cumulative dose of irradiation. Five patients also provided samples 6 months after the therapy. Hyposalivation or xerostomia occurred in all patients, although the pretreatment secretion rates were already relatively low. Salivary amylase activities decreased with increasing dose of radiation, especially when expressed as the amount of enzyme secreted per minute. Unusually high salivary concentrations of albumin, lactoferrin, lysozyme, salivary peroxidase, myeloperoxidase, and total protein were observed during the therapy, but most values slowly returned to pretreatment levels after cessation of radiation. It is concluded that the observed qualitative changes in whole saliva components are net effects caused by the cancer itself, radiation therapy given, systemic diseases, or medications, as well as mucosal inflammations.
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PMID:Changes in the protein composition of whole saliva during radiotherapy in patients with oral or pharyngeal cancer. 242 87

The effects of timolol maleate on the secretion and composition of human saliva were studied in vivo. Eight healthy volunteers received orally 10 mg timolol maleate. Stimulated parotid saliva samples, resting whole saliva samples, and blood samples were collected immediately before and four times after the drug intake at intervals of 1 h. The levels of total protein, lysozyme, IgA, IgG and IgM, salivary peroxidase, myeloperoxidase, lactoferrin, amylase, thiocyanate (SCN-), and hypothiocyanite (OSCN-) were analyzed from saliva samples. Drug levels were measured both from parotid saliva and blood samples. Results were compared to the analyses of the samples collected in a similar way but without administration of any drugs. Decreased levels of total protein, lactoferrin, amylase, and salivary peroxidase were observed in parotid saliva after a single oral dose of timolol maleate. No such decrease was found in lysozyme, myeloperoxidase, SCN-, OSCN-, or immunoglobulins. Salivary flow rate was not significantly changed after drug intake. The results suggest that the beta-blocking drug may cause qualitative changes in the composition of saliva by inhibiting the synthesis and/or release of acinar proteins.
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PMID:Effects of a beta-blocking agent, timolol maleate, on saliva in healthy volunteers. 245 Dec 71

EDTA inhibits the formation of I3- from iodide catalysed by various pure peroxidases. The inhibition is concentration-dependent and chloroperoxidase (CPO) is more sensitive than horseradish peroxidase (HRP) and lactoperoxidase (LPO). EDTA is more active than EGTA or other biological chelators tested. Zn2+, Mn2+ and Co2+ are equally active in reversing the effect of EDTA on both CPO and HRP almost completely, but ineffective in the case of LPO. The effect of EDTA on HRP can be reversed by a higher concentration of iodide but not by H2O2. EDTA causes a hypsochromic change in the absorption of the Soret band of HRP at 402 nm, and iodide can reverse this effect. EDTA can effectively displace radioiodide specifically bound to HRP. It is suggested that EDTA inhibits iodide oxidation by interacting at the iodide binding site of the HRP.
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PMID:EDTA inhibits peroxidase-catalyzed iodide oxidation through interaction at the iodide binding site. 250 57

Peroxidases belong to a group of enzymes which catalyze the oxidation of numerous organic and inorganic substrates by hydrogen peroxide. Most peroxidases, including lactoperoxidase (LPO), contain ferriprotoporphyrin IX as a prosthetic group. A characteristic feature of hemoprotein peroxidases is their ability to exist in various oxidation states. There are five known enzyme intermediates. In increasing order of their oxidative equivalents these are ferrous enzyme, ferric or native enzyme, Compound II, Compound I, and Compound III (sections 5, 7). They are readily distinguished from each other by their absorbance in the Soret region (380-450 nm) and visible range (450-650 nm). In the course of Compound III and Compound II conversion back to the native peroxidase, oxygen derived free radicals such as O2-, HO.2, and .OH are generated. Simultaneously the enzyme is irreversibly damaged. In the presence of an exogenous electron donor, such as iodide, the interconversion between the various oxidation states of the peroxidase is markedly affected. Compound II and/or Compound III formation is inhibited, depending on the H2O2 concentration. In addition, the enzyme is largely protected from irreversible inactivation. These effects of iodide are readily explained by 1) the two-electron oxidation of iodide to Iox by Compound I, which bypasses Compound II as an intermediate, and 2) the rapid oxidation of H2O2 to O2 by the oxidized species of iodide which prevents the generation of oxygen derived free radicals.
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PMID:Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals. 254 51

The interaction of aromatic donor molecules with lactoperoxidase (LPO) was studied using 1H-NMR and optical difference spectroscopy techniques. pH dependence of substrate proton resonance line-widths indicated that the binding was facilitated by protonation of an amino acid residue (with pKa of 6.1) which is presumably a distal histidine. Dissociation constants evaluated from both optical difference spectroscopy and 1H-NMR relaxation measurements were found to be an order of magnitude larger than those for binding to horse radish peroxidase (HRP), indicating relatively weak binding of the donors to LPO. The dissociation constants evaluated in presence of excess of I- and SCN- showed a considerable increase in their values, indicating that the iodide and thiocyanate ions compete for binding at the same site. The dissociation constant of the substrate binding was, however, not affected by cyanide binding to the ferric centre of LPO. All these results indicate that the organic substrates bind to LPO away from the ferric center. Comparison of the dissociation constants between the different substrates suggested that hydrogen bonding of the donors with the distal histidine amino acid, and hydrophobic interaction between the donors and the active site contribute significantly towards the associating forces. Free energy, entropy and enthalpy changes associated with the LPO-substrate equilibrium have been evaluated. These thermodynamic parameters were found to be all negative and relatively low compared to those for binding to HRP. The distances of the substrate protons from the ferric center were found to be in the range 9.4-11.1 A which are 2-3 A larger than those reported for the HRP-substrate complexes. These structural informations suggest that the heme in LPO may be more deeply buried in the heme crevice than that in the HRP.
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PMID:Binding of aromatic donor molecules to lactoperoxidase: proton NMR and optical difference spectroscopic studies. 254 4

The binding of thiocyanate to lactoperoxidase (LPO) has been investigated by 1H and 15N NMR spectroscopy. 1H NMR of LPO shows that the major broad heme methyl proton resonance at about 61 ppm is shifted upfield by addition of the thiocyanate, indicating binding of the thiocyanate to the enzyme. The pH dependence of line width of 15N resonance of SC15N- in the presence of the enzyme has revealed that the binding of the thiocyanate to the enzyme is facilitated by protonation of an ionizable group (with pKa of 6.4), which is presumably distal histidine. Dissociation constants (KD) of SC15N-/LPO, SC15N-/LPO/I-, and SC15N-/LPO/CN- equilibria have been determined by 15N T1 measurements and found to be 90 +/- 5, 173 +/- 20, and 83 +/- 6 mM, respectively. On the basis of these values of KD, it is suggested that the iodide ion inhibits the binding of the thiocyanate but cyanide ion does not. The thiocyanate is shown to bind at the same site of LPO as iodide does, but the binding is considerably weaker and is away from the ferric ion. The distance of 15N of the bound thiocyanate ion from the iron is determined to be 7.2 +/- 0.2 A from the 15N T1 measurements.
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PMID:Binding of thiocyanate to lactoperoxidase: 1H and 15N nuclear magnetic resonance studies. 254 89

A perfused rat liver took up bovine lactoperoxidase (LPO) by a Ca2+-dependent, saturable process. This endocytosis was accomplished by both hepatocytes and Kupffer or other nonparenchymal cells (NPCs). The mediating receptors were the Gal/GalNAc lectin of hepatocytes and the Man/GlcNAc lectin of NPCs. Blocking either one of these receptors caused a large shift in distribution of accumulated LPO into the cell type whose receptor was left unblocked, but the extent of uptake was unaffected and the rate was only moderately reduced. Effective inhibition of overall uptake into the perfused organ required the presence of competitors for both receptors. Conversely, LPO was an effective competitor of other ligands (asialoorosomucoid or mannan) for either of the two receptors. The major clearance capacity for LPO was associated with hepatocytes which in suspension took it up by a process completely inhibitable by asialofetuin (ASF) and at a rate more than three times greater than for ASF. A faster cycling time for Gal/GalNAc receptors when bound to LPO is suggested. The glycoprotein selectively lost its affinity for Man/GlcNAc receptors when digested by endoglycosidase H (endo H), suggesting that LPO contains mannose-rich oligosaccharides.
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PMID:Endocytosis of bovine lactoperoxidase by two carbohydrate-specific receptors in rat liver. 257 66

Because early childhood is an important period for the colonization of bacteria in the primary dentition, it is possible that antimicrobial factors in saliva may modify these early events. In this study we have followed longitudinally 33 children from predentate to dentate phase and analyzed whole saliva for such salivary factors as lysozyme, lactoferrin, salivary peroxidase, myeloperoxidase, thiocyanate, hypothiocyanite, total IgA, IgG, IgM, and total protein. Children's saliva samples were compared with those from an adult reference group whose samples were collected and analyzed in an identical way. It was observed that salivary thiocyanate and IgG increased and salivary peroxidase decreased significantly from predentate to dentate phase. The other parameters remained unchanged. Children in predentate phase already had reached adult levels of hypothiocyanite and IgM, whereas all the other components were found in significantly lower amounts in children's saliva than in adult saliva. Salivary myeloperoxidase assay is interfered by the thiocyanate ions, and the observed increase in salivary "myeloperoxidase" activity may be due to the simultaneous increase in salivary thiocyanate.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Antimicrobial factors in whole saliva of human infants: a longitudinal study. 262 37

Resonance Raman (RR) spectra of hog thyroid peroxidase (TPO) were observed for the first time and compared with those of lactoperoxidase (LPO) and horseradish peroxidase (HRP). Since TPO purified by monoclonal antibody-assisted immunoaffinity chromatography was strongly fluorescent, the surface enhancement technique using Ag colloid adsorption was used for the oxidized form, but ordinary RR spectra could be obtained for the reduced form. The RR spectra of TPO were distinct from those of HRP in both the oxidized and reduced states and indicated the presence of six-coordinated iron-protoporphyrin.
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PMID:Resonance Raman characterization of hog thyroid peroxidase. An SERRS study. 272 78

On the basis of optical difference spectra, lactoperoxidase (LPO) was shown to form a 1:1 complex with aromatic donor molecules: resorcinol, hydroquinone, phenol, p-cresol, guaiacol, aniline, and benzohydroxamic acid. As compared with horseradish peroxidase (HRP), the values of the dissociation constant, Kd, of LPO-donor complexes were found to be 4-720-fold larger and were not greatly changed in the presence of KCN and by changes in pH in the range 4-9. The apparent enthalpy and entropy of the binding reactions were found to be -13 kJ mol-1 and -29 J mol-1 K-1, respectively, somewhat smaller (in absolute value) than the corresponding values of HRP. The difference spectra of LPO-donor complexes resembled each other, in contrast to the case of HRP, and the bindings of the donors to LPO occurred in a competitive fashion between the donors. Incubation of LPO with phenylhydrazine and hydrogen peroxide markedly depressed donor binding, the intensity of the Soret band, and the catalytic activity, probably as the result of formation of meso-phenyl derivatives of the heme. These findings suggest that the binding of aromatic donors to LPO occurs at a specific site, probably near the heme edge, where the electron transfer in the peroxidase reaction may take place.
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PMID:Interaction of aromatic donor molecules with lactoperoxidase probed by optical difference spectra. 273 Aug 81


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