Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.11.1.7 (peroxidase)
65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adhesion of artificially generated lipid membrane vesicles to Chinese hamster V79 fibroblasts in suspension was used as a model system for studying membrane interactions. Below their gel-liquid crystalline phase transition temperature, vesicles comprised of dipalmitoyl lecithin (DPL) or dimyristoyl lecithin (DML) absorbed to the surfaces of EDTA- dissociated cells. These adherent vesicles could not be removed by repeated washings of the treated cells but could be released into the medium by treatment with trypsin. EM autoradiographic studies of cells treated with[(3)H]DML or [(3)H]DPL vesicles showed that most of the radioactive lipids were confined to the cell periphery. Scanning electron microscopy and fluorescence microscopy further confirmed the presence of adherent vesicles at the cell surface. Adhesion of DML or DPL vesicles to EDTA-dissociated cells modified the lactoperoxidase-catalyzed iodination pattern of the cell surface proteins; the inhibition of labeling of two proteins with an approximately 60,000- dalton mol wt was particularly evident. Incubation of cells wit h (3)H-lipid vesicles followed by sodium dodecyl sulfate (SDS)- polyacrylamide gel electrophoresis showed that some of the (3)H-lipid migrated preferentially with these approximately 60,000-mol wt proteins. Studies of the temperature dependence of vesicle uptake and subsequent release by trypsin showed that DML or DPL vesicle adhesion to EDTA- dissociated cells increased with decreasing temperatures. In contrast, cells trypsinized before incubation with vesicles showed practically no temperature dependence of vesicle uptake. These results suggest two pathways for adhesion of lipid vesicles to the cell surface-a temperature-sensitive one involving cell surface proteins, and a temperature-independent one. These findings are discussed in terms of current models for cell-cell interactions.
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PMID:Adhesion of phospholipid vesicles to Chinese hamster fibroblasts. Role of cell surface proteins. 40 33

Alterations in cell surface glycoproteins have been implicated in malignancy. We examined surface membrane proteins of a cultured cell line, SKCO-1, which had been derived from a human colonic adenocarcinoma. Cell surface labeling of SKCO-1 cells with galactose oxidase, followed by reduction with sodium borotritide, revealed five major labeled glycoproteins upon sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. At least three additional labeled glycoproteins could be detected if galactose oxidase treatment was preceded by neuraminidase treatment. Some, but not all, of the glycoproteins could be iodinated by lactoperoxidase. The predominantly labeled glycoprotein (GPI) had a molecular weight of 200,000 and co-migrated in SDS gel with carcinoembryonic antigen (CEA). GPI was not removed from the cell surface by EDTA, hypertonic saline, or sonication but was released from the membrane by detergents. This glycoprotein was subsequently purified using lectin-agarose columns and gel filtration. GPI was judged homogenous by protein- and carbohydrate-stained SDS-polyacrylamide gels and had an amino acid composition similar to that of CEA. The carbohydrate composition of GPI was qualitatively similar to CEA but quantitatively distinct. GPI had a greater proportion of sialic acid and galactosamine and less fucose and glucosamine than CEA. Immunological studies, however, demonstrated identity between GPI and CEA. A study of the turnover rate of GPI showed it to have a half-life of 5 days.
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PMID:Glycoproteins from human colonic adenocarcinoma. Isolation and characterization of cell surface carcinoembryonic antigen from a cultured tumor cell line. 41 28

Little is known about the factors controlling somatostatin secretion in man, and data are not available on the changes in circulating levels in various human physiological or pathophysiological states. This is mainly a consequence of the technical difficulties involved in measuring somatostatin in plasma. In the presence of plasma, binding of somatostatin tracer to antibody was consistently decreased by about 20%, and this could not be abolished by the addition of EDTA and aprotinin or by the use of specially prepared somatostatin-free plasma. Furthermore, in the presence of plasma, endogenous somatostatin does not dilute in parallel with synthetic cyclic somatostatin standard. We have, therefore, developed and validated a radioimmunoassay for somatostatin using prior extraction of the peptide onto leached silica glass. Tyrosine-II somatostatin was iodinated using lactoperoxidase and purified on ODS silica. This method is superior to iodination using chloramine-T with CMC cellulose purification, and gives a highly purified preparation with a shelf-life of at least eight weeks. Using this tracer and a specific antiserum, the limit of sensitivity of the assay was 10 pg/ml, with an intra-assay coefficient of variation of 12% (n = 16) and inter-assay coefficient of variation of 15% (n - 10). Parallelism has been demonstrated between standard synthetic cyclic somatostatin and all extracted plasma samples. The mean recovery of exogenous somatostatin from plasma was 78%. The fasting level of immunoreactive somatostatin at 0,900 hours in 40 normal subjects ranged from 17 to 81 pg/ml. Care is needed, however, when comparing these values with those obtained from other laboratories since standard preparations of somatostatin vary considerably in their immunopotency.
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PMID:Development and validation of a specific radioimmunoassay for somatostatin in human plasma. 42 Apr 98

Cytochrome b-562.5 (Ulva pertusa) was extracted from a green alga, U. pertusa, by homogenization of the thalli in phosphate buffer solution. Purification was carried out by acrinol treatment, ammonium sulfate fractionation, DEAE-cellulose and DEAE-Sephadex column chromatographies, and Sephadex gel filtration. Cytochrome b-562.5 has absorption maxima at 562.5 (alpha), 530.5 (beta), 429 (gamma), and 326 nm (delta) in the reduced form and at 537, 415 (gamma), and 275 nm in the oxidized form. The alpha-band of the reduced form is asymmetric with a shoulder at 560 nm, at liquid nitrogen temperature this band splits into two distinct peaks at 562 and 556.5 nm. The absorption maxima of the pyridine ferrohemochrome appear at 556 (alpha), 523 (beta), and 418 nm (gamma). The cytochrome does not combine with carbon monoxide or cyanide. The preparation of the cytochrome shows little peroxidase activity. The cytochrome is oxidized by ferricyanide and reduced by cysteine, ascorbate, and hydrosulfite. Autoxidation of the cytochrome was found to be very slow. The midpoint potential (Em) of the cytochrome was determined by equilibration with the ferro- and ferri-EDTA system to be +0.20 V at pH7.0. The molecular weight of the cytochrome was estimated by Sephadex gel filtration to be 23x10(3).
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PMID:Purification and properties of cytochrome b-562.5 from Ulva pertusa. 42 58

The decarboxylation of retinoic acid by horseradish peroxidase was investigated. A marked increase in the yield of products was obtained. However, the data indicated the reaction was a nonenzymatic, heme catalyzed peroxidation. Previously reported requirements for phosphate, oxygen and ferrous ion were eliminated when hydrogen peroxide was provided. Peroxide also eliminated the EDTA and cyanide induced inhibition of the phosphate dependent system. In the presence of hydrogen peroxide, horseradish peroxidase was not essential to the reaction; heme equivalent amounts of hemoglobin decarboxylated retinoic acid with equal facility. However, hemoglobin was ineffective in the absence of hydrogen peroxide. Attainment of 50--60% decarboxylation represented complete utilization of the available retinoic acid. Thus the products of the reaction can be divided into two groups, products of retinoic acid oxidation and products of an oxidative decarboxylation of retinoic acid.
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PMID:The oxidation and decarboxylation of retinoic acid by horseradish peroxidase. 47 30

Platelet satellitosis resulted in an elevated high-peroxidase-activity value (9.9% versus normal range 0 to 3.65%) of the automated leukocyte differential count performed by the Technicon Hemalog D. Platelet satellitism occurred in Wright-stained smears of EDTA-anticoagulated blood, as well as in the effluent of the peroxidase channel of the Hemalog D. All platelets took up the perosidase stain. The rosette-like clusters of platelets and neutrophils were interpreted as single, large, intensely stained leukocytes resulting in the elevated high-peroxidase-activity value.
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PMID:Platelet satellitism as a cause of abnormal hemalog D differential results. 60 12

Arachidonic acid (AA) is the essential substrate for production of platelet endoperoxides and thromboxanes. Iron or heme is an essential cofactor for the peroxidase, lipoxygenase and cyclo-oxygenase enzymes involved in formation of these products. The present study has examined the direct interactions between iron and arachidonic acid. Iron caused the oxidation of AA into more polar products which could be detected by UV absorbtion at 232 nM or the thiobarbituric acid (TBA) reaction. High pressure liquid chromatography, chem-ionization and electron-impact mass spectrometry and nuclear magnetic resonance spectroscopy suggest that the major product was a hydroperoxide of AA. Ferrous iron (Fe++) and oxygen were absolute requirements. Fe++ was converted to the ferric iron (Fe+++) state during oxidation of AA, but Fe+++ could not substitute for Fe++. No other enzymes, cofactors or ions were involved. Conversion of AA to a hydroperoxide by Fe++ was inhibited by the antioxidant, 2, (3)-Tert-butyl-4-hydroxyanisole, the radical scavenger, nitroblue tetrazolium, and iron chelating agents, including EDTA, imidazole and dihydroxybenzoic acid. The reaction was not affected by superoxide dismutase, catalase or aspirin. These findings and preliminary studies of the Fe++ induced oxidation product of AA as a substrate for prostaglandin synthesis and inhibitor of prostacyclin production indicate the critical role of Fe++ in AA activation.
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PMID:The role of iron in prostaglandin synthesis: ferrous iron mediated oxidation of arachidonic acid. 71 48

The plasmalemma and hyaline ectoplasm together constitute the sensory and motor organ of macrophages. The purpose of this study was to isolate this cell fraction in order to analyze it biochemically and functionally. Brief sonification of warmed rabbit lung macrophages caused release of heterodisperse hyaline blebs and filopodia, which were easily collected by differential centrifugation. Viewed in the electron microscope, these structures consisted of membrane-bounded sacs principally containing actin filaments. Some contained secondary lysosomes. They were enriched threefold over whole cell homogenates in specific adenylate cyclase activity and in trichloroacetic-acid-precipitable (125)I when derived from cells labeled with 125(I) by means of a lactoperoxidase-catalyzed reaction. These markers were found to have identical isopycnic densitites when macrophage homogenates were subjected to sedimentation in a focusing sucrose density gradient system, and these markers had densities distinct from those of other cytoplasmic organelles. These markers were therefore assumed to be associated with macrophage plasma membranes. The specific beta- glucuronidase activity of the bleb fraction was similar to that of homogenates, but the blebs had considerably lower specific succinic dehydrogenase activity and RNA content, and DNA was undetectable. Electrophoresis of blebs solubilized in sodium dodecyl sulfate on polyacrylamide gels revealed polypeptides co-migrating with macrophage actin-binding protein, myosin, and actin; blebs also had EDTA-activated adenosine triphosphatase activity characteristic of myosin. The concentrations of actin-binding protein and myosin were higher in blebs than in cells or cytoplasmic extracts, whereas actin concentrations were similar (relative to extracts) or only slightly greater (than in cells). Blebs and intact cells had high lactate dehydrogenase activities in the presence but not the absence of Triton X-100. Blebs and cells oxidased 1-[(14)C]glucose, and the rate of glucose oxidation was increased substantially in the presence of latex beads. We conclude that intact sacs of plasmalemma encasing contractile proteins and cytoplasmic enzymes can be isolated from macrophages. They are enriched in myosin and actin-binding protein, indicating that the contractile apparatus is regulated in the cell periphery. These structures have the capacity to respond to environmental signals. We suggest the name "podosomes" for them because of their resemblance to macrophage pseudopodia. We propose that podosome formation results from rapid dissolution of the cortical gel when the membrane is in an actively extended configuration.
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PMID:Peripheral hyaline blebs (podosomes) of macrophages. 92 88

Lactoperoxidase, in the presence of H2O2, I-, and rat liver microsomes, will peroxidize membrane lipids, as evidenced by malondialdehyde formation. Fe3+ assists in the formation of malondialdehyde. Fe3+ can be added at the end of the reaction period as well as at the beginning with equal effectiveness, suggesting that it only acts to assist in the conversion of lipid peroxides, previously formed by lactoperoxidase, to malondialdehyde. The addition of EDTA to the microsomal reaction mixture results in a 40% decrease in malondialdehyde formation. The antioxidant butylated hydroxytoluene will completely block the formation of malondialdehyde. Malondialdehyde formation is not dependent upon the production of superoxide, singlet oxygen, or hydroxyl radicals. Peroxidation of membrane lipids by this system is equally effective in both intact microsomes and in liposomes, indicating that iodination of microsomal protein is not required for lipid peroxidation to occur.
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PMID:Lactoperoxidase-catalyzed lipid peroxidation of microsomal and artificial membranes. 98 86

The reduction of oxygen by irradiated chloroplasts was studied for elucidation of oxygen action site in the electron transport chain of photosynthesis. Chemiluminescence system, consisted of luminol and peroxidase, was used for registration of oxygen reduction products. In the first case chemiluminescence system was added to supernatant fraction after centrifugation of suspension of irradiated chloroplasts in order to determine H2O2 which was found to be the final product of oxygen photoreduction. In the second case when chloroplasts were illuminated in the presence of chemiluminescence system and oxygen the fact delayed luminescence of luminol was observed. This photoluminescence related also with the oxygen reduction in chloroplasts caused a possible formation of radicals HO2 (or -O2). The formation of this radicals and H2O2 was inhibited by DCMU, heating of chloroplasts at 45 degrees C for 5 min and by washing with EDTA and NH2OH. The rate of HO2 dissappearance was increased by methylviologen. The kinetics of photoluminescence of luminol and afterglow of chlorophyll in chloroplasts was identical in the interval from 20 msec to several seconds. It is suggested that oxygen reaction site is located near the reaction centre of chloroplasts.
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PMID:[Study of oxygen photoreduction in chloroplasts by the method of luminol and chlorophyll chemiluminescence]. 120 56


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