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)

A cysteine protease has been purified from bloodstream forms of Trypanosoma congolense by affinity chromatography on cystatin-Sepharose. A polyclonal antibody was raised against the purified enzyme and used for immunocytochemical localization of the enzyme by electron microscopy. Antibody labeling of the cysteine protease, using colloidal gold-labeled protein A (PrA-Au), was observed over amorphous material within subcellular organelles which have the appearance of lysosome-like bodies. This intracellular labeling colocalized in organelles containing bovine serum albumin-gold (BSA-Au) that had been endocytosed by the living parasites. The PrA-Au/antibody also labeled the flagellar pocket and parasite cell surface, albeit less consistently. Volume density analysis showed that the organelles containing endocytosed BSA-Au, after 30 min incubation at 37 degrees C in BSA-Au, comprised approximately 22% of the total parasite cell volume. Under similar conditions, but employing horseradish peroxidase (HRP) as a fluid-phase marker of the lysosomal system, only 5.7% of the cell contained HRP. This value dropped to 3.6% after 60 min incubation. Volume density analysis showed that the amorphous material which was labeled by the antibody to the cysteine protease occupied 6.9% of the cell volume. This amorphous material was contained within a membrane-bound lysosome-like organelle that occupied 11.5% of the cell. Thus, the cysteine protease appears to be present in half, or less, of the lysosomal system of T. congolense.
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PMID:Immunolocalization of a cysteine protease within the lysosomal system of Trypanosoma congolense. 180 11

The anti-diquat (DQ) monoclonal antibodies with high specificity were produced. An immunogen was synthesized by binding DQ to bovine serum albumin via a diazo-coupled intermediate. BALB/c mice were injected intraperitoneally once a month with 0.25 mg of the immunogen for 5 months. Their spleen cells were fused with P3U1 myeloma cells to get hybridoma clones secreting anti-DQ antibodies. Two anti-DQ monoclonal antibodies (ADM-1, ADM-2) were subtyped to be IgM and IgG3, respectively. A competitive ELISA was developed with ADM-2. More than 0.05 micrograms of DQ was measured without any interference from human serum. The ADM-2 showed high affinity for DQ and no cross-reactivities with paraquat and other analogues. DQ in sera of poisoning patients were successfully determined by the ELISA. On the other hand, the ADM-2 was applicable to the immunohistochemical demonstration of DQ distribution in experimental animals. An avidin-biotin-peroxidase complex method was used in this immunohistochemical study. DQ-intoxicated rats were killed at 3 h, 12 h, 24 h, 3 days and 7 days after intravenous administration of DQ (30 mg/kg). The macrophages containing DQ in the lung started to be observed at 12 h after injection and the number increased till 7 days. From 3 hours after injection, DQ was localized in the epithelial cells of the distal tubules and collection tubules, but not in the glomeruli in the kidney. In the heart, at every time from 3 h to 7 days after DQ administration, a few myocardial cells were positive with the immunohistochemical staining. The ADM-2 was expected to be available in practice of forensic and analytical toxicology.
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PMID:[Production of monoclonal antibody against diquat and its application for forensic medicine]. 181 Nov 7

Drugs which compete with bilirubin for albumin binding may increase the risk of kernicterus. Fortunately, few drugs are strong competitors. However, in neonatology, many drugs are used simultaneously. We have studied the effect of drug combinations on bilirubin binding using human serum albumin and the peroxidase method. Combinations of aminophylline with phenobarbital, cefotaxime and vancomycin were studied as well as the combination of vancomycin and cefotaxime. The results show that the bilirubin-displacing effect of the drug combinations cannot be predicted from each drug's individual effect. These results are consistent with a flexible model of albumin binding. Combinations of drugs which are both albumin-bound and reach high serum concentrations should be tested for their combined effect on bilirubin binding and this information used in deciding on treatment in sick, premature infants.
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PMID:Effect of drug combinations on bilirubin-albumin binding. 181 27

Interleukin 1 alpha and beta are polypeptide cytokines that possesses a wide variety of immunologic and inflammatory activities. We have examined the role of intrapulmonary interleukin 1 in the pathogenesis of acute IgG immune complex alveolitis in the rat. Intratracheal instillation of IgG anti-bovine serum albumin accompanied by intravenous infusion of bovine albumin results in acute neutrophil and complement-dependent alveolitis. Over the course of evolving lung injury there was a 12-fold increase in bronchoalveolar lavage fluid interleukin 1 activity. Intratracheal instillation of neutralizing anti-interleukin 1 beta antibodies upon induction of lung injury resulted in a dose-dependent reduction in lung injury as assessed by measurements of pulmonary hemorrhage and vascular permeability. Morphometric analysis and measurements of myeloperoxidase activities in whole lung homogenates from rats that received anti-interleukin 1 beta revealed a pronounced reduction in neutrophil recruitment compared to positive controls. Incubation of isolated alveolar macrophages with preformed IgG immune complexes resulted in dose-dependent interleukin 1 secretion. These data suggest that intrapulmonary IL-1 activity plays a role in neutrophil recruitment and is necessary for the full development of acute IgG immune complex induced lung injury in the rat.
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PMID:Intrapulmonary interleukin 1 mediates acute immune complex alveolitis in the rat. 182 36

We have compared the role of tumor necrosis factor (TNF) in the pathogenesis of analogous acute immune complex-induced lung and dermal vascular injury models in rats. Intratracheal administration of IgG anti-bovine serum albumin (BSA), followed immediately by intravenous infusion of BSA, results in acute neutrophil-mediated alveolitis. Neutralization of intrapulmonary TNF activity with anti-TNF antibodies resulted in reduced pulmonary neutrophil recruitment and marked attenuation of lung injury. Intradermal injection of IgG anti-BSA, followed by intravenous BSA, results in acute neutrophil-mediated dermal vasculitis. Neither locally nor systemically administered anti-TNF antibodies reduced dermal vascular injury as measured by local hemorrhage and vasopermeability changes. Based on morphometric analysis and measurements of myeloperoxidase in tissue extracts, anti-TNF antibodies had no effect on dermal neutrophil recruitment. Intradermal and intrapulmonary administration of physiologic concentrations of recombinant human TNF resulted in modest, dose-dependent increases in local vasopermeability accompanied by negligible neutrophil recruitment. Administration of higher concentrations of TNF resulted in increases in both local vasopermeability and neutrophil recruitment. These data suggest that while both rat pulmonary and dermal blood vessels can respond to TNF-triggered proinflammatory events, endogenous TNF plays a much greater role in acute alveolitis than in dermal vasculitis.
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PMID:Disparate roles for TNF in the pathogenesis of acute immune complex alveolitis and dermal vasculitis. 183 7

Because 17 beta-19-nortestosterone and its esters are frequently used anabolic steroids in cattle in Europe, there is a need for an assay that can also detect certain metabolites. The enzyme immunoassay described here involves the detection and quantitation of the major metabolite 17 alpha-19-nortestosterone in urine. The assay is based on the coating of an antibody raised in a rabbit against 17 alpha-19-nortestosterone-3-carboxy-methyloxime-bovine serum albumin (17 alpha-19-NT-3-CMO-BSA), the competitive incubation of 17 alpha-19-NT and the 17 alpha-19-nortestosterone-3-CMO-horseradish peroxidase label, followed by the detection of the blue colour developed by the action of the enzyme on tetramethylbenzidine. The 3-CMO conjugate of 17 alpha-19-nortestosterone was used to produce an antibody with selective affinity for the 17 alpha-epimer. For the optimization of the assay, different coatings and incubation conditions were tested. The standard curve ranged between 0.98 and 4000 pg per well, with a B/B0 50% of +/- 65 pg per well. Colour was measured with a microtitre plate reader. The method was validated by means of certified blank and spiked cattle urine samples.
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PMID:Development of a competitive enzyme immunoassay for 17 alpha-19-nortestosterone. 187 49

The localization of meprobamate-like (MPB-like) molecules in the neuromuscular junction of rats has been investigated at light- and electron- microscopic levels with the peroxidase-antiperoxidase (PAP) immunohistochemical method, using a purified antiserum obtained from rabbits immunized with a meprobamate-bovine serum albumin (MPB-BSA) conjugate. The immunoreaction was found surrounding synaptic vesicles and in protuberant deposits situated in the post-synaptic membrane. These facts suggest the existence of endogenous MPB-like molecules in neuromuscular junction and that the immunostained protuberant deposits should mark the receptors of those molecules.
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PMID:Presence of meprobamate-like molecules in rat neuromuscular junction. Immunohistochemical demonstration at light- and electron-microscopic levels. 187 23

Polyethylene glycol (PEG)-oxirane was synthesized by reacting aminated monomethoxy-PEG 5000 (NH2-MPEG 5000) with butanediol diglycidyl ether and used to derivatize bovine serum albumin (BSA) and monoclonal antibodies (mAb) against horseradish peroxidase (HRP) and porcine lactate dehydrogenase isoenzyme 5, respectively. Determination of oxirane end groups revealed a very high number, which arise from the chain breaks of the polymer. Covalent coupling of PEG-oxirane to BSA resulted in 30-50 times higher partition coefficients under optimized conditions. The mAb investigated could be modified with PEG-oxirane while retaining its binding properties and could be used as an affinity ligand for selective extraction of Ag in immunoaffinity partitioning. However, a high degree of modification results in a lower binding constant of mAb anti-HRP and higher [mAb]/[Ag] concentration ratios in immunoaffinity partition experiments.
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PMID:Immunoaffinity partitioning: synthesis and use of polyethylene glycol-oxirane for coupling to bovine serum albumin and monoclonal antibodies. 188 29

A recent paper (Buchberger, W., 1988, J. Chromatogr. 432, 57) on lactoperoxidase-catalyzed bromination of tyrosine and thyroglobulin stated, without evidence, that thyroid peroxidase (TPO) is able to use bromide as a substrate. This was in disagreement with unpublished experiments previously performed in this laboratory, and we undertook, therefore, to examine this subject further. Highly purified porcine TPO was compared with lactoperoxidase (LPO) and chloroperoxidase (CPO) for ability to catalyze bromination of tyrosine, thyroglobulin, and bovine serum albumin (BSA). The incubation mixture contained 50-100 nM peroxidase, 10-500 microM 82Br-, tyrosine (150 microM), thyroglobulin (0.3 or 1 microM), or BSA (7.5 microM), and a source of H2O2. The latter was either generated by glucose (1 mg/ml)-glucose oxidase (0.5 or 1 micrograms/ml), or added initially as a bolus (100 microM). With TPO, formation of organically bound 82Br was undetectable under all conditions in the pH range 5.4-7.0. Lactoperoxidase and CPO, on the other hand, displayed considerable brominating activity. Lactoperoxidase was much more active at pH 5.4 than at pH 7.0 and was more active with BSA as acceptor than with tyrosine or thyroglobulin. The distribution of 82Br among the various amino acids in LPO-brominated thyroglobulin and BSA was determined by HPLC. As expected, monobromotyrosine and dibromotyrosine together comprised the greatest part of the bound 82Br. However, a surprisingly high percentage (20-25%) was present as monobromohistidine. Evidence was also obtained for the presence of a small percentage of the bound 82Br as tetrabromothyronine. Peroxidase-catalyzed bromination probably depends on the oxidation of Br- to Br+ by the Compound I form of the enzyme. Since oxidation of Br- to Br+ requires a stronger oxidant than oxidation of I- to I+, our results suggest that Compound I of LPO and of CPO has a higher oxidation potential than Compound I of TPO. In vivo experiments with rats on a low iodine diet injected with 82Br- showed that even under conditions of high stimulation by thyrotropic hormone, there is negligible formation of organic bromine in the thyroid. Measurements of thyroid:serum concentration ratios for 82Br- in similar rats provided no evidence that Br- is a substrate for the iodide transport system of the thyroid.
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PMID:Peroxidase-catalyzed bromination of tyrosine, thyroglobulin, and bovine serum albumin: comparison of thyroid peroxidase and lactoperoxidase. 189 6

We have developed a sensitive and rapid solid-phase assay for the serum enzyme UDPGal:beta-D-GlcNAc beta-1,4-galactosyltransferase (beta 1,4-GT) (EC 2.4.1.38) that employs the recombinant bioluminescent protein aequorin as the enzyme label for product detection. The substrate for beta 1,4-GT is a neoglycoprotein, bovine serum albumin containing covalently attached GlcNAc residues (GlcNAc-BSA), and it was immobilized by adsorption in microtiter plate wells. Serum samples were added to each well along with saturating levels of UDPGal and Mn2+. Galactosylation of the neoglycoprotein acceptor by the serum beta 1,4-GT produces the N-acetyllactosamine derivative Gal beta 1, 4GlcNAc-BSA. The product formed is quantified by adding the biotinylated plant lectin Ricinus communis agglutinin-I, which binds specifically to N-acetyllactosamine, followed by the addition of streptavidin and the biotinylated aequorin. Aequorin produces a flash of light in response to Ca2+ and is detectable to 10(-19) mol in a luminometer. Using this assay, the beta 1,4-GT activity in human serum and the activity of a semipurified beta 1,4-GT are linear with time and serum concentration over a wide range. The reaction is dependent on UDPGal and Mn2+, is highly reproducible with a low background, and can be performed in a few hours. Assays employing aequorin have a wider range of linearity than those employing horseradish peroxidase as an enzyme label. These results demonstrate that the assay for beta 1,4-GT is useful for determining activity in heterogeneous samples and also demonstrate the utility of the recombinant protein aequorin for solid-phase assay methods.
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PMID:A solid-phase assay for beta-1,4-galactosyltransferase activity in human serum using recombinant aequorin. 190 13


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