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At least 19 recordsLinked to original sources
PubMed1977

On the molecular composition and physico-chemical properties of the pseudo-exfoliation material.

The protein tracer peroxidase has been found to be excluded from pseudoexfoliation (PE) material. But after the treatment of the PE material with cetylpyridinium-chloride, peroxidase was found to penetrate into the material. This observation seems to support the concept that the PE material is a gel of proteoglycans, from which peroxidase is excluded by an excluded volume effect. Microperoxidase was found to penetrate into the superficial parts of the (untreated) PE material, and to be regularly distributed according to two different patterns: 1) along the PE fibrils, and 2) along lines in the interfibrillar matrix; lines which can not be seen without the presence of microperoxidase. At both locations the microperoxidase reaction product was found at regular intervals, with spacings of about 53 nm. The interpretation is that both the fibrils and the interfibrillar matrix are composed of the same kind of long extended linear proteoglycan complexes, but with a different arrangement and density.

Eye Diseases↗
PubMed1978

Chloroperoxidase-catalysed oxidation of 4-chloroaniline to 4-chloronitrosobenze.

The incubation of 4-chloroaniline with chloroperoxidase and H2O2 resulted in a rapid formation of 4-chloronitrosobenzene. This enzymic oxidation displayed a pH optimum at 4.4 with a Km of 8.1x10(-4)M and catalytic-centre activity of 312. The initial rate of the reaction was strongly affected by the presence of halide ions. 4-Chlorophenylhydroxylamine was even more rapidly converted into the nitroso compound. A reaction mechanism is proposed on the basis of currently accepted theory for the catalytic action of chloroperoxidae. A noteworthy aspect of this new reaction is the difference in the products previously reported for the action of classical peroxidases on anilines and the single nitroso product resulting from chloroperoxidase oxidation.

Aniline Compounds↗
PubMed1975

Chloroperoxidase: P-450 type absorption in the absence of sulfhydryl groups.

The oxidation state of the two half-cystine residues in the native ferric form of chloroperoxidase and in the reduced ferrous chloroperoxidase has been examined in order to evaluate the role of sulfhydryl groups as determinants of P-450 type spectra. Mössbauer and optical spectroscopy studies indicate that the ferrous forms of P-450cam and chloroperoxidase have very similar or identical heme environments. Model studies have suggested that sulfhydryl groups may function as axial ligands for developing P-450 character. However, chemical studies involving both sulfhydryl reagents and amperometric titrations show that neither the ferric nor the chemically produced ferrous forms of chloroperoxidase contain a sulfhydryl group. These results rule out the hypothesis that sulfhydryl groups are unique components for P-450 absorption characteristics. The optical and electron paramagnetic resonance (EPR) spectra of the nitric oxide complex of chloroperoxidase have been obtained and compared to those of myoglobin, hemoglobin, and cytochrome c and horseradish peroxidase. The EPR spectrum of the NO-ferrous chloroperoxidase complex, which is similar to that of cytochrome P-450cam, does not show the extra nitrogen hyperfine structure which appears to be characteristic of those hemoproteins which have a nitrogen atom as an axial heme ligand.

Chemical Phenomena↗
PubMed1976

Peroxidase-catalyzed halogenation.

Peroxidase-catalyzed halogenation reactions have been established as being important in the biosynthesis of the hormone thyroxine and in biological defense mechanisms. Recently these reactions have been recognized as valuable tools for the study of proteins as well as their arrangement in macromolecular structures. The pathways of peroxidase catalyses can be accommodated within the framework of the classical Chance-George mechanism. This implies that the initial steps of the reaction invariably involve oxidation of peroxidases by peroxides--and that the resulting derivative, compound I, is the oxidant of the halide ions. Such reactions may result either in the formation of hypohalous acids, or in halogenation of the enzyme apoprotein, followed by transhalogenation to substrate for halogenation. Chloro- and myeloperoxidases catalyze oxidation of all halide ions, except F-; oxidation of bromide and iodide is mediated by lactoperoxidase, but horseradish peroxidase only oxidizes iodide. All of the above enzymes except horseradish will oxidize the pseudo halide thiocyanate. The origins of this differentiation remain to be defined, but they presumably reflect significant variation in oxidation potential of different peroxidase-peroxide derivatives, rather than constraints on the peroxidase-donor interactions. As pointed out above, halogenation of the amino acids tyrosine and histidine or these residues in proteins can take place on the enzyme. This makes lactoperoxidase-catalyzed iodination selective. The amino acid residues in proteins that are iodinated depend not only on reactivity of the amino acid residue but also on its geometric location. Thus lactoperoxidase-catalyzed iodination can be a useful tool in the study of protein structure and function. It is also useful in establishing the geometric position of proteins within macromolecular structures. Thyroid peroxidase catalyzes iodination of thyroglobulin and is involved in a second important step, the coupling of the iodotyrosines to form thyroxine or triiodothyronine. A proposed mechanism for this reaction suggests that the oxidation is mediated by the iodoenzyme derivative mentioned above followed by a prototropic rearrangement and scission to form the ether bound of thyronine and a serine residue on thyroglobulin.

Amino Acids↗
PubMed1979

Antithyroid and antiperoxidase activity of tropolone and 3-hydroxy-4-pyrone.

Tropolone (TR) and 3-hydroxy-4-pyrone were investigated for antithyroid activity following the finding that the 2-hydroxy-oxo pyridine, 3-hydroxy-4(1H)-pyridone (DHP, I), is goitrogenic. Both compounds inhibited the thyroidal uptake of radioiodine in rats and resembled the thioamide drugs in inhibiting the organic binding of iodine by the thyroid gland rather than the trapping of iodide, but were weaker binding inhibitors than 6-methyl-2-thiouracil (MeTU). Both compounds also inhibited the iodination of bovine serum albumin and thyroglobulin, catalyzed by thyroidperoxidase (TPO), lactoperoxidase (LPO), chloroperoxidase (CPO) and horseradish peroxidase (HPO) in vitro. The inhibitory effect of TR but not that of 3-hydroxy-4-pyrone was antagonized by ferrous ions. When fed to mice at levels of intake expected to produce goitre both compounds were toxic and caused severe liver damage. Thyroid enlargement was not observed in any of these feeiding experiments, but the thyroids of mice fed 0.1% TR showed moderate hyperplasia. It was concluded that both compounds are weakly goitrogenic. Hyperactivity was observed in the mice fed TR which may be associated with inhibition of catechol methyl transferase (COMT).

Animals↗
PubMed1979

Resonance Raman investigations of chloroperoxidase, horseradish peroxidase, and cytochrome c using Soret band laser excitation.

Resonance Raman spectra of the heme protein chloroperoxidase in its native and reduced forms and complexed with various small ions are obtained by using laser excitation in the Soret region (350-450 nm). Additionally, Raman spectra of horseradish peroxidase, cytochrome P-450cam, and cytochrome c, taken with Soret excitation, are presented and discussed. The data support previous findings that indicate a strong analogy between the active site environments of chloroperoxidase and cytochrome P-450cam. The Raman spectra of native chloroperoxidase are found to be sensitive to temperature and imply that a high leads to low spin transition of the heme iron atom takes place as the temperature is lowered. Unusual peak positions are also found for native and reduced chloroperoxidase and indicate a weakening of porphyrin ring bond strengths due to the presence of a strongly electron-donating axial ligand. Enormous selective enhancements of vibrational modes at 1360 and 674 cm-1 are also observed in some low-spin ferrous forms of the enzyme. These vibrational frequencies are assigned to primary normal modes of expansion of the prophyrin macrocycle upon electronic excitation.

Binding Sites↗
PubMed1979

Peroxide oxidation of indole to oxindole by chloroperoxidase catalysis.

In the presence of chloroperoxidase, indole was oxidized by H2O2 to give oxindole as the major product. Under most conditions oxindole was the only product formed, and under optimal conditions the conversion was quantitative. This reaction displayed maximal activity at pH 4.6, although appreciable activity was observed throughout the entire pH range investigated, namely pH 2.5-6.0. Enzyme saturation by indole could not be demonstrated, up to the limit of indole solubility in the buffer. The oxidation kinetics were first-order with respect to indole up to 8 mM, which was the highest concentration of indole that could be investigated. On the other hand, 2-methylindole was not affected by H2O2 and chloroperoxidase, but was a strong inhibitor of indole oxidation. The isomer 1-methylindole was a poor substrate for chloroperoxidase oxidation, and a weak inhibitor of indole oxidation. These results suggest the possibility that chloroperoxidase oxidation of the carbon atom adjacent to the nitrogen atom in part results from hydrogen-bonding of the substrate N-H group to the enzyme active site.

Catalysis↗
PubMed1977

In vitro stability and in vivo clearance of fibrinogen or serum albumin labeled with 77Br, 131I, or 125I by direct or indirect synthetic methods.

Conventional protein iodination involves the addition of an oxidizing agent to the protein solution. Through the use of the acylating agent N-succinimidyl-3(4-hydroxyphenyl)propionate, labeling can be accomplished without subjecting the protein to oxidizing conditions. Fibrinogen and serum albumin labeled with 131I and 77Br by this technique were compared with each other and with 125I-protein prepared by direct iodination using the ICI, chloramine-T, and lactoperoxidase methods. Iodinated proteins have two drawbacks: the high radiation dose accompanying 125I and 131I, and the ease of hydrolysis of the weak carbon-iodine bond. These drawbacks can be overcome by using 56-hr 77Br.

Acylation↗
PubMed1978

Studies on the ultrastructure and permeability of the hemotrichorial placenta. II. Fetal capillaries and tracer administration into the fetal blood circulation.

The distribution of horseradish peroxidase and lanthanum chloride within the full term chorioallantoic placenta of the rat was examined after administration of these tracers into the umbilical artery. Both tracers rapidly traverse the capillary endothelium. Transendothelial channels, fenestrations and micropinocytotic vesicles provide the main pathways. Intercellular clefts which are either patent or interrupted by leaky intercellular junctions, also contribute to a rapid passage of low and high molecular weight substances. Deep channel-like invaginations, effecting an increase of the exchange area of layer III, are freely accessible to the tracers from the interspace between the capillary endothelium and trophoblastic layer III. The invaginations, however, are not in continuity with the interspace between layers II and III, verifying the syncytial character of layer III. Neither an uptake of the tracers nor a passage across layer III is observed. The main permeability barrier to feto-maternal transfer within the chorioallantoic placenta is localized in the syncytiotrophoblastic layer III. This layer controls the passage of low molecular weight substances and restricts the penetration of high molecular weight substances.

Animals↗
PubMed1978

Studies on the ultrastructure and permeability of the hemotrichorial placenta. I. Intercellular junctions of layer I and tracer administration into the maternal compartment.

The distribution of lanthanum chloride and horseradish peroxidase within the full-term chorioallantoic placenta of the rat was investigated 1 to 20 min after administration of these tracers into the maternal blood circulation. Both tracers rapidly penetrate trophoblastic layer I and diffuse into the interspace between layers I and II. They are localized in extensive infoldings and caveolae of the outer surface of layer II. The syncytial character of layer II is confirmed at this development stage of the placenta. There is no vesicular uptake or penetration beyond layer II until 20 min after tracer administration. Our results indicate that trophoblastic layer II is the main barrier in the chorioallantoic rat placenta preventing the permeation of macromolecules from maternal to fetal compartments. With freeze-fracturing, particulate strutures of variable arrangement and size are found between adjacent cells of layer I. With goniometric analysis small gaps between the appositions of the membrane are observed. These structures are interpreted as tight and/or gap junctions during stages of assembly or disassembly.

Animals↗
PubMed1975

Effect of cadmium chloride on the rat testicular soluble selenoenzyme, glutathione peroxidase.

Thirty-six hours after male rats were injected with 25 mumoles cadmium chloride/ml/kg of body weight they exhibited decreased plasma and testicular glutathione (GSH) peroxidase activity, testicular atrophy and necrosis, and increased testicular thiobarbituric acid-reactive products. Seven days after injection, only the plasma GSH peroxidase activity returned to normal. The decrease in testicular GSH peroxidase activity was not reversible by dialysis against buffer or by the addition of selenium as buffered selenomethionine. In vitro inhibition of testicular GSH peroxidase activity occurred at 0.3 mM cadmium. All in vivo effects were prevented by a prior injection of 25 mumoles sodium selenite/ml/kg of body weight. Testicular GSH peroxidase may be the direct or indirect target of cadmium-induced testicular damage, and this damage results in lipid peroxidation.

Animals↗
PubMed1979

Horseradish peroxidase. XXXIV. Oxidation of compound II to I by periodate and inorganic anion radicals.

The one-electron oxidation of horseradish peroxidase compound II to compound I by sodium periodate was observed. The bimolecular rate constant for the NaIO4--compound II interaction is equal to 9.5 +/- 1 x 10(-3) M-1s-1 at room temperature. Irradiation, using ultraviolet light, of the solution containing compound II and persulfate in the presence of bicarbonate, chloride, or bromide, leads ot the fast accumulation of compound I due to the oxidative action of SO4, CO3, Cl2, and Br2 anion radicals, which are products of the photolysis.

Bicarbonates↗
PubMed1976

Compound X. An intermediate in enzymatic halogenation.

Previous studies have shown that chlorite serves as a halogenation substrate for horseradish peroxidase. In its substrate role, chlorite serves both as a halogen donor and as a source of oxidizing equivalents in the chlorination reaction. We now show that a new spectral intermediate, which we have termed Compound X, can be detected as the initial product of the reaction of chlorite with horseradish peroxidase. The reaction of chlorite with horseradish peroxidase to form Compound X is a relatively fast reaction especially at acidic pH values. The second order rate constant (Kf) for the formation of Compound X at pH 4.5 (optimum pH) is 0.9 X 10(6) M-1 S-1. Compound X, in the absence of a halogen acceptor, decomposes to Compound I and chloride ion. The first order rate constant (Kd) for the decay of Compound X to Compound I is 0.2 s-1 at pH 4.5. The pH optimum for enzymatic chlorination with chlorite compares favorably with the pH profile for the lifetime of Compound X (Kf/Kd). These observations indicate that Compound X is the halogenating intermediate in the chlorite reaction and that the rate of enzymatic chlorination is directly related to the stability of Compound X. We propose an -OCl ligand on a ferric heme as the most likely structure for Compound X.

Binding Sites↗
PubMed1978

The effects of various stimuli on the cellular composition of peritoneal exudates in the mouse.

A comparative study on the composition of cell populations collected from the unstimulated mouse peritoneal cavity and at various intervals after the intraperitoneal injection of glycerol trioleate, casein, paraffin oil, glycogen, sodium chloride, and proteose peptone, was carried out. The cellular composition of the peritoneal exudates, especially with respect to the ratio of monocytes to resident macrophages, was shown to be dependent on the nature of the stimulus and interval after stimulation.

Animals↗