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 direct enzyme immunoassay was developed to measure conjugated oestrogens in the plasma of pregnant mares. The antibody was produced in rabbits using oestrone-3-glucuronide (E1G) conjugated to bovine serum albumin. The enzyme conjugate was E1G conjugated to horseradish peroxidase. A sharp increase in plasma E1G concentrations occurred between Days 35 and 40 of gestation. Values declined slightly to Day 45, remained relatively constant to around Day 70 and rose sharply thereafter. Fetal death before Day 35 had no effect on plasma concentrations of E1G. Fetal death after Day 35 in conjunction with endotoxin-induced regression of the corpus luteum (CL) resulted in a decrease in plasma E1G levels to non-pregnant values within 3-4 days. Endotoxaemia without fetal death between Days 35 and 70 resulted in marked, but transient, decreases in plasma E1G concentrations. Fetal death without CL regression after Day 35 did not produce an immediate decline in plasma E1G concentrations and existing levels were maintained for 10-14 days. These findings indicate that between Days 35 and 70 of pregnancy, plasma E1G concentrations are not directly correlated with fetal viability; they appear to reflect increased oestrogen secretion by the CL under the influence of chorionic gonadotropin. After Day 70, E1G concentrations begin to reflect directly the production of oestrogen by the developing feto-placental unit.
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PMID:An oestrogen conjugate enzyme immunoassay for monitoring pregnancy in the mare: limitations of the assay between days 40 and 70 of gestation. 166 16

An immune complex transfer enzyme immunoassay for (anti-human T-cell leukemia virus type I) IgG (anti-HTLV-I IgG) in serum using a synthetic peptide, cys-gag p19(100-130), is described. Anti-HTLV-I IgG in test serum, which had been incubated with excess of inactive beta-D-galactosidase to eliminate interference by anti-beta-D-galactosidase antibodies, was reacted simultaneously with 2,4-dinitrophenyl bovine serum albumin-cys-gag p19(100-130) conjugate and cys-gag p19(100-130)-beta-D-galactosidase conjugate. The complex formed of the three components was trapped onto polystyrene balls coated with affinity-purified (anti-2,4-dinitrophenyl group) IgG. After washing to eliminate nonspecific IgG in the test serum and excess of the beta-D-galactosidase conjugate, the complex was eluted from the polystyrene balls with epsilon N-2,4-dinitrophenyl-L-lysine and transferred to polystyrene balls coated with affinity-purified (anti-human IgG gamma-chain) IgG. Beta-D-Galactosidase activity bound to the (anti-human IgG gamma-chain) IgG-coated polystyrene balls was assayed by fluorometry. This assay was 100-fold more sensitive than the conventional enzyme immunoassay, in which a cys-gag p19(100-130)-bovine serum albumin-coated polystyrene ball was incubated with test serum and, after washing, with (anti-human IgG gamma-chain) Fab'-peroxidase conjugate. The degree of inhibition by preincubation of test sera with excess of cys-gag p19(100-130) in combination with an appropriate cut-off value for the fluorescence intensity of bound beta-D-galactosidase activity discriminated almost all seropositive samples from seronegative ones.
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PMID:Immune complex transfer enzyme immunoassay for (anti-human T-cell leukemia virus type I) IgG in serum using a synthetic peptide, Cys-Gag p19(100-130), as antigen. 168 32

The hybrid hybridomas (tetradomas) were produced from the fusion of the double mutant actinomycin Dr (ADr)/HATs hybridoma to horseradish peroxidase (HRP) and wild type hybridoma to alpha-endorphin (EP). The double mutant phenotype was constructed using the new strategy, based on the fusion of immune mouse splenocytes with mouse myeloma (X63.Ag8, 653) cell variants, made resistant to 30 ng/ml of AD by stepwise selection. This allowed the direct introduction of the dominant selective marker (ADr) into the hybrid cells. Tetradomas secreted the bispecific monoclonal antibodies (bi Mabs), simultaneously binding to EP and HRP in double antigen ELISA, the ELISA plates covered with EP-bovine serum albumin conjugate. Using rat pituitary the bi Mabs were shown to be effective for immunostaining of EP-producing cells. EP-producing cells.
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PMID:[A new approach to the design of hybrid hybridomas based on the use of an actinomycin D-resistant line of murine myeloma]. 168 61

The kinetics of iodinated human alpha-fetoprotein (AFP) binding and uptake by 2 human neoplastic lymphoid cell lines (CEM and RAJI) have been studied. Three saturation plateaus were obtained by incubating CEM and RAJI cells at 4 degrees C with 125I-AFP at different concentrations. Scatchard analysis suggested the presence of 3 types of receptor site with different affinities and capacities on cells of both lines. AFP binding was inhibited by unlabelled human and bovine AFP, and to a lesser extent by human serum albumin (SAH); no significant competition was observed with human transferrin (Tf) or ovalbumin (Ova). Pulse-chase experiments showed that 125I-AFP was released practically undegraded from the cells. Covalent conjugates of AFP and Tf with horseradish peroxidase (HRP) were used to follow the endocytosis and intracellular pathway of these serum proteins by electron microscopy. Both proteins were observed in coated vesicles, endosomes and a tubular vesicular network localized in the Golgi-centrosphere region. SAH-HRP was internalized to a much lesser extent. Ova-HRP was poorly internalized and was observed in lysosome-like organelles.
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PMID:Receptor-mediated endocytosis and recycling of alpha-fetoprotein in human B-lymphoma and T-leukemia cells. 170 4

Antiserum raised against horseradish peroxidase (HRP) recognizes a neural specific carbohydrate antigen in Drosophila and other insects. The epitopic activity of the carbohydrate moiety of HRP recognized by anti-HRP antiserum was measured by a newly developed enzyme-linked immunosorbent assay, in which HRP glycopeptides conjugated with bovine serum albumin were coated onto the wells and then reacted with goat anti-HRP antiserum. HRP sugar moieties released by almond glycopeptidase A digestion of HRP pepsin digests were subjected to pyridylamination. Pyridylamino oligosaccharides were separated into seven fractions by reverse-phase high performance liquid chromatography. The major fraction, which comprised about 80% of the total sugars, reacted strongly with anti-HRP antiserum. The carbohydrate structure of this fraction was determined by sugar composition analysis and 600-MHz 1H NMR spectroscopy as follows: Man alpha 1----6(Man alpha 1----3)(Xyl beta 1----2)Man beta 1----4GlcNAc beta 1----4(Fuc alpha 1----3)GlcNAc. Analyses of reactivity with anti-HRP antiserum of various oligosaccharide derivatives obtained from the major fraction by exoglycosidase digestion and partial acid hydrolysis indicated that alpha 1----6-linked mannose and alpha 1----3-linked fucose are predominantly involved in the epitopic structure.
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PMID:The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. 170 47

In view of the likelihood that the heparin-binding growth factors of fibroblast growth factors are neurotrophic for the neurones of the chick ciliary ganglion a study has been made of the retrograde axonal transport of the acidic and basic fibroblast growth factors by these neurones. No high capacity retrograde axonal transport of these molecules was seen. The amount of transport was equivalent to the low level seen with many proteins such as horse radish peroxidase or bovine serum albumin rather than the convincing transport seen for nerve growth factor in the sympathetic system. The iodinated proteins retained their ability to bind to neuronal receptors. Thus, if the fibroblast growth factors are neurotrophic in the ciliary ganglion, they may exert their action by mechanisms other than the retrograde axonal transport of the factor itself.
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PMID:Lack of retrograde axonal transport of the heparin-binding growth factors by chick ciliary neurones. 171 48

The ability of the trophoblast of the ovine preimplantation blastocyst to take up and metabolise proteins has been investigated using two experimental approaches, microscopical and radiochemical. The ultrastructure of the expanded blastocyst obtained from 14 and 17 day pregnant ewes was examined. The morphology of tissues maintained in culture for 24 h has been compared with that of fresh tissues. After culture, the cellular morphology of the explants was well preserved. Fresh and 24 h cultured tissues were incubated with horse-radish peroxidase and ferritin and these proteins subsequently were found to be localized in coated pits, caveolae and secondary lysosomes of the trophoblast. Comparison of the uptake of [3H]dextran and of 125I-labelled bovine serum albumin indicated that proteins could be taken up by cultured tissue by mechanisms in addition to simple fluid phase endocytosis. During culture of explants of blastocyst with 125I-labelled bovine serum albumin, a large fraction of the radioactivity taken up by the tissue appeared in the TCA-soluble fraction of the culture medium indicating that cultured trophoblast hydrolysed proteins. That amino acids released from captured protein could be used for protein synthesis by the trophoblast was indicated by the labelling of tissue and medium proteins after culturing explants with beta-lactamase labelled with [14C]leucine. A major product (Mr approximately 17 x 10(3) present in the medium was likely to have been ovine trophoblast protein-1. It is concluded that, during the expansion of the ovine blastocyst, the trophoblast has the ability to take up proteins, transport them to lysosomes and degrade them to amino acids which are used for protein synthesis. Thus proteins, as well as free amino acids, present in the histotrophe may be an important source of nitrogen for the sheep conceptus in the critical period just prior to implantation.
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PMID:Morphological and radiochemical evidence for the metabolism of exogenous proteins by the preimplantation sheep blastocyst. 172 46

We increased selectivity in the detection of glycoproteins on nitrocellulose membranes by introducing a washing step using sodium hydroxide solution. Glycoproteins on the nitrocellulose membrane were first oxidized by sodium periodate; biotin hydrazide was then coupled to the aldehyde groups generated in the sugar moiety of the glycoproteins. The membrane was washed twice using sodium hydroxide solution, and avidin-horseradish peroxidase was then coupled to the remaining biotin. This system allows the detection of nanograms of glycoproteins on nitrocellulose membranes, and its specificity allows the clear distinction of glycoproteins from the nonglycosylated protein of bovine serum albumin.
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PMID:Increased selectivity in the detection of glycoproteins on nitrocellulose membranes by washing with sodium hydroxide solution. 175 55

Tuberculoventral neurons in the deep layer of the dorsal cochlear nucleus (DCN) provide frequency-specific inhibition to neurons in the anteroventral cochlear nucleus (AVCN) of the mouse (Wickesberg and Oertel, '88, '90). The present experiments examine the projection from the deep DCN to the posteroventral cochlear nucleus (PVCN). Horseradish peroxidase (HRP) injections into the PVCN reveal that the multipolar cell area, but not the octopus cell area, is innervated by neurons in the deep layer of the DCN. Injections into the multipolar cell area, in the rostral and ventral PVCN, labeled neurons across the entire rostrocaudal extent of the deep DCN. The labeled tuberculoventral neurons generally lay within the band of labeled auditory nerve terminals in the DCN. Injections of HRP into the octopus cell area, in the dorsal caudal PVCN, labeled almost no cells within the band of auditory nerve fiber terminals that were labeled by the same injection. The inhibition from tuberculoventral neurons onto ventral cochlear nucleus (VCN) neurons is likely to be mediated by glycine (Wickesberg and Oertel, '90). Slices of the cochlear nuclear complex were immunolabeled by an antibody against glycine conjugated with glutaraldehyde to bovine serum albumin (Wenthold et al., '87). Glycine-like immunoreactivity was found throughout the DCN, the AVCN and the multipolar cell area, but there was little labeling in the octopus cell area. This finding provides independent evidence that tuberculoventral neurons do not innervate the octopus cell area and indicates that the octopus cell area is anatomically and functionally distinct.
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PMID:Tuberculoventral neurons project to the multipolar cell area but not to the octopus cell area of the posteroventral cochlear nucleus. 177 Jan 69

Enzyme-linked immunosorbent assays for bovine alpha-lactalbumin and beta-lactoglobulin have been developed for measurements of serum and tissue culture samples. Either alpha-lactalbumin or beta-lactoglobulin antiserum was coated on ELISA plates. Biotinylated proteins were used in competition with unknown amount of proteins in samples. After unbound proteins were washed off, ExtrAvidin-peroxidase and tetramethylbenzidine were then used as a detection system. Crossreactivity of caseins or bovine serum albumin was less than .0001% in either alpha-lactalbumin or beta-lactoglobulin ELISA. Parallel curves from serial dilutions were obtained in serum and media samples. The additivity of alpha-lactalbumin and beta-lactoglobulin ELISA was validated in either serum or medium samples. The intraassay and interassay coefficients of variation for alpha-lactalbumin and beta-lactoglobulin ELISA were below 10% over 51 and 47 assays. The ELISA are useful in mammary gland biology studies for measuring milk whey protein in serum or culture media.
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PMID:Enzyme-linked immunosorbent assays for bovine alpha-lactalbumin and beta-lactoglobulin in serum and tissue culture media. 177 50


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