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)

Plasma membranes from chick embryo neuronal primary cultures were isolated after subjecting 5-day-old cells, previously surface labeled with either lactoperoxidase-catalyzed radioiodination or galactose oxidase/NaB3H4, to a freeze-thaw cycle. The cellular material adhering to the culture substratum was washed, and the "wash" fractions were pooled and centrifuged at 37,000g. The resulting pellet was resuspended in 3 ml of buffer, layered on 33 ml of 33% sucrose, and centrifuged at 105,000g. Radioactivity was recovered at the top of the gradient. Sedimentation of these fractions and biochemical studies revealed that the pellet was 20- and 12-fold enriched in (Na+,K+)-adenosinetriphosphatase and 5'-nucleotidase, respectively. The preparation was devoid of inner mitochondrial (succinate dehydrogenase), outer mitochondrial (monoamine oxidase), endoplasmic reticulum (glucose-6-phosphatase), outer mitochondrial (monoamine oxidase), endoplasmic reticulum (glucose-6-phosphatase), and Golgi (UDP galactose:N-acetylglucosamine galactosyltransferase) enzymatic markers. Ultrastructural studies showed that the membrane preparation was homogeneous and lacked mitochondria endoplasmic reticulum and lysosomes. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate showed the presence of 11 protein components with molecular masses ranging from 120 to 300 kDa. This method for the isolation of plasma membranes probably depends on the capacity of the cellular material to adhere to the culture substratum and to entrap intracellular organelles during the freeze-thaw cycle. The membrane preparation seems suitable for studying the function of high-molecular-weight protein components of neuronal plasma membranes.
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PMID:Isolation of plasma membranes from neurons grown in primary culture. 282 51

1. Propylthiouracil (PTU) was degraded by myeloperoxidase (MPO) or eosinophil peroxidase (EPO), purified from rat bone marrow, in the presence of H2O2 and Cl-. In the absence of either H2O2 or Cl-, MPO and EPO do not degrade PTU. Optimum concentrations of KCl for MPO and EPO were 50 and 250 mM, respectively. 2. The characteristics of PTU degradation by MPO-H2O2-Cl- were similar to those of the chlorinating activity of the peroxidase. 3. Hypochlorous acid as well as MPO-H2O2-Cl- also degraded PTU. Metabolites of PTU degradation by MPO-H2O2-Cl-, which were separated by C18 reversed phase h.p.l.c., were the same as those produced by hypochlorous acid. 4. Of the metabolites of PTU formed by MPO-H2O2-Cl-, one was identified as PTU sulphonic acid (6-propyl-4-hydroxypyrimidine-2-sulphonate) and another seemed to be propyluracil.
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PMID:Oxidative metabolism of propylthiouracil by peroxidases from rat bone marrow. 285 96

P beta (color opponent) retinal ganglion cells in macaques were found to degenerate as a result of oral administration of acrylamide. Histological examination, wheat germ agglutinin-horseradish peroxidase transport and cytochrome oxidase histochemistry indicate that other retinal ganglion cells and other neurons in the visual pathways were spared.
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PMID:Selective acrylamide-induced degeneration of color opponent ganglion cells in macaques. 301 58

Since the mechanisms that control synthesis of surface and internal granule membranes are closely-related within the Golgi apparatus, we have compared the plasma membrane proteins and glycolipids of cells of the human promyelocytic line HL-60 with those of its agranular myeloblastoid variant (HL60-D), and of other human myeloid lines (KG-1a, KG-1 and ML-2). Proteolytic degradation by granule enzymes altered the protein profiles unless multiple inhibitors were included in the cell suspension before lysis and during subsequent handling of the extracts. Polyacrylamide gel electrophoretic profiles of the proteins accessible to lactoperoxidase-catalyzed 125I-labeling or to periodate [3H]-borohydride labeling, as well as those of the glycoproteins bound to and eluted from immobilized concanavalin A, showed distinct patterns. The apparent molecular weights of the two major sialylated glycoproteins were larger in cell lines with a greater content of azurophilic granules. Also, the blastic line incorporated less fucose into glycolipid and contained less complex gangliosides and neutral glycolipids than did the parent. These data demonstrate that, within the limits of this culture model, cells capable of cytoplasmic granule production express a different constellation of surface components.
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PMID:Differences in the plasma membrane glycoproteins of cultured myeloblastoid and promyelocytic human leukemia (HL60) cells. 301 85

Various methods of radioiodination were employed to identify peptides on the surface of Dirofilaria immitis microfilariae. Optimum surface radiolabelling occurred with the lactoperoxidase-catalyzed reaction. Two major peptides of 16 and 14 kDa were labelled by this method. These peptides were soluble in Nonidet P-40, were not glycosylated, and showed no signs of disulfide linkages. These peptides were immunoprecipitated by sera from D. immitis-infected dogs, but not by sera from uninfected dogs or sera from dogs with potentially cross-reactive nematode infections. Analysis of the 14 and 16 kDa peptides by two-dimensional gel electrophoresis revealed that the 16 kDa peptide was a single unit with a pI of 5.25 whereas the 14 kDa band was composed of three individual peptides with pI values ranging from 5.6 to 6.1. Iodination by chloramine T resulted in the same panel of labelled peptides but suffered from poor efficiency of 125I incorporation. The viability of microfilariae labelled by the standard Bolton-Hunter method decreased by 50% following the reaction which resulted in the labelling of a variety of internal components.
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PMID:Antigenic peptides on the surface of Dirofilaria immitis microfilariae. 308 56

A sensitive and specific method has been developed for analyzing specific antibody clonotype changes during an immune response or comparing multiple sera for antibody clonotype similarities. Polyclonal serum antibodies were separated by flatbed acrylamide isoelectric focusing (IEF) and analyzed by an affinity immunoblotting method using antigen-coated nitrocellulose membranes. Antibodies present on the surface of the acrylamide gels after IEF bound the antigen on the nitrocellulose when the coated nitrocellulose was laid over the gels. Non-specific protein binding was inhibited with Tween 20. Bound IgG antibody clonotypes were detected using peroxidase-conjugated anti-IgG. This method has been used for the analysis of Ig clonotypes specific for five protein antigens and two carbohydrate antigens. Optimal antigen concentration for coating the nitrocellulose membranes ranged from 10 to 100 micrograms/ml. The reactions could be inhibited by saturating the nitrocellulose with soluble protein antigen or free hapten prior to immunoblotting. Antibodies of alternative allotypic forms were detected by probing the immunoblot with biotinylated anti-allotype antibodies instead of anti-IgG. The simultaneous analysis of alternative allelic forms of antibodies of defined specificity is not possible with methods which use labelled antigen for clonotype detection.
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PMID:Affinity immunoblotting. High resolution isoelectric focusing analysis of antibody clonotype distribution. 353 39

Two variants of B16 mouse melanoma cells, selected for their resistance to toxic levels of wheat germ agglutinin isolectin 1 (WGA-1) in serum-free medium, showed by chromosome analysis that they are still mouse cell-lines, continue to produce melanin, and are less tumorigenic in mice than the parent B16 cells. The variants showed a marked decrease in cell agglutination with the wheat germ lectin and a slight increase in cell agglutination with concanavalin A. The binding of 125I-labeled wheat germ agglutinin to the two variant lines was likewise decreased over a 10(3)-fold range of lectin concentrations. Terminal sialyl residues were critical in WGA-1 binding to the wild-type cells. The binding data indicated a decrease in high-affinity binding as well as a decrease in the total number of binding sites in the variants. Polyacrylamide gel electrophoresis, followed by affinity staining with 125I-wheat germ agglutinin, showed alterations in the wheat germ agglutinin-binding glycoproteins in the variants compared to those of the parent cell line. However, lactoperoxidase-catalyzed iodination revealed a similar cell-surface protein pattern among the three cell lines. Radioactive glycoproteins secreted or shed by the three cell lines grown in the presence of [3H]glucosamine in serum-free medium were fractionated on the basis of their interaction with WGA-Sepharose (2 mg/mL). The WGA-bound glycoproteins from the two variants had molecular weights of 92,000, 56,000, and 42,000. None of these components was detected in the parent cell-line. A major WGA-binding glycoprotein, which accounted for 37% of the total [3H]glucosamine incorporated, was isolated from the spent medium of the parent mouse melanoma cell-line. This glycoprotein was apparently absent in the WGA-1-resistant variants.
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PMID:Characteristics of two wheat germ agglutinin-resistant variants of B16 mouse melanoma cells with reduced tumorigenicity. 376 99

A peroxidase saturation technique for the determination of coating antigen concentration necessary to saturate polystyrene plates with a wide range of different antigens is described. The same technique has also been used to compare the stability of antigen-polystyrene bonds for native and denaturated antigens. Furthermore, the inappropriate selection of solid-phase antigen concentration and its influence on ELISA results is analyzed and an experimental criterion to select the optimum antigen concentration is proposed. Two different antigens, BSA-Ar and hydatid antigen, were used for ELISA determination of specific antibodies as a model system. Optimum solid-phase antigen concentration was determined by two different methods: peroxidase saturation, in which binding of peroxidase to non-antigen-occupied polystyrene surface sites was used to evaluate the degree of coating by antigen; chequer-board titration, using several immune sera of different affinity. Optimum antigen concentration selected by chequer-board titration using low affinity sera was similar to that selected with peroxidase saturation. On the other hand, lower antigen concentration would be selected by chequer-board titration using high affinity sera. For this reason, the concentrations of low affinity antibodies would be underestimated using the chequer-board titration. These results indicate that peroxidase saturation should be used to avoid avidity-dependent artifacts in ELISA.
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PMID:New experimental criteria for optimization of solid-phase antigen concentration and stability in ELISA. 378 6

Acrylamide (ACR) produces a central-peripheral distal axonopathy, via an unknown mechanism. We have investigated the effects of ACR on the activity of enzymes responsible for the oxidation of NADH (NADH-tetrazolium reductase activity, NADH-TR) with quantitative histochemical techniques. Chronic (5- or 10-day) injection of ACR (50 mg/kg/day) resulted in a significant decrease in enzyme activity in soleus motoneurons, which normally have high NADH-TR activity. The NADH-TR activity in motoneurons with low oxidative metabolism was not significantly affected. Retrograde labeling of motoneurons with horseradish peroxidase was diminished by the acrylamide treatment. These data demonstrate an acrylamide-induced change in the oxidative metabolism of certain motoneurons; further study will determine whether oxidative metabolism is the primary site of action of ACR in producing the distal axonopathy.
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PMID:Acrylamide alters oxidative enzyme activity in rat motoneurons. 403 5

The enzyme lactoperoxidase (iodide:hydrogen-peroxide oxidoreductase, EC 1.11.1.8) was used to iodinate ((125)I) accessible proteins on membranes of intact virally transformed and untransformed cells. A number of labeled bands of proteins were detected by acrylamide gel electrophoresis. A heavily labeled band with a molecular weight of approximately 250,000 daltons was found in all untransformed cells but was absent from transformed cells. When Coomassie-blue-stained membrane preparations were compared, a band was seen in normal cells which co-migrated with the lactoperoxidase-labeled band. In transformed cell membranes, three discrete bands were present in the same position. Thus, the expression of this protein may be altered when cells are in the transformed state.
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PMID:A comparison of membrane proteins of normal and transformed cells by lactoperoxidase labeling. 436 Sep 46


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