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HRP

The emission yield from the horseradish peroxidase (HRP)-catalyzed luminol oxidations can be kicreased as much as a thousandfold upon addition of substituted phenols, eg, -iodophenol, -phenylphenol, or 6-hydroxybenzothiazole (119). Enhanced chemiluminescence, as this phenomenon is termed, has been the basis for several very sensitive immunometric assays that surpass the sensitivity of radioassay (120) techniques and has also been developed for detection of nucleic acid probes ia dot-slot. Southern, and Northern blot formats (121). [Pg.268]

A method of detecting herbicides is proposed the photosynthetic herbicides act by binding to Photosystem II (PS II), a multiunit chlorophyll-protein complex which plays a vital role in photosynthesis. The inhibition of PS II causes a reduced photoinduced production of hydrogen peroxide, which can be measured by a chemiluminescence reaction with luminol and the enzyme horseradish peroxidase (HRP). The sensing device proposed combines the production and detection of hydrogen peroxide in a single flow assay by combining all the individual steps in a compact, portable device that utilises micro-fluidic components. [Pg.332]

The extent to which the nature of the task could allow the hazard to cause harm to workers, the public or the environment (hazard release potential., HRP)... [Pg.211]

Therefore, the effective isotropic spin Hamiltonian for the radical pair Hrp is given by equation (21). [Pg.70]

Neuroanatomists have taken advantage of the phenomenon of fast retrograde transport to locate remote nerve cell bodies in the CNS of an experimental animal that are connected to an identified axonal fiber tract whose origin is uncertain. The tracer material [purified horseradish peroxidase (HRP) enzyme] is injected in the region of the axon terminals, where it is taken up by endocytosis and then is carried by retrograde axonal transport over a period of several hours to days back to the nerve cell body. The animal is sacrificed, and the enzyme tracer is localized by staining thin sections of the brain for peroxidase activity. [Pg.15]

Phenol, the simplest and industrially more important phenolic compound, is a multifunctional monomer when considered as a substrate for oxidative polymerizations, and hence conventional polymerization catalysts afford insoluble macromolecular products with non-controlled structure. Phenol was subjected to oxidative polymerization using HRP or soybean peroxidase (SBP) as catalyst in an aqueous-dioxane mixture, yielding a polymer consisting of phenylene and oxyphenylene units (Scheme 19). The polymer showed low solubility it was partly soluble in DMF and dimethyl sulfoxide (DMSO) and insoluble in other common organic solvents. [Pg.229]

The control of the polymer structure was achieved by solvent engineering. The ratio of phenylene and oxyphenylene units was strongly dependent on the solvent composition. In the HRP-catalyzed polymerization of phenol in a mixture of methanol and buffer, the oxyphenylene unit increased by increasing the methanol content, while the buffer pH scarcely influenced the polymer structure. ... [Pg.229]

The polymerization outcome depended on the monomer structure as well as on the enzyme origin. For instance, using HRP and p-n-alkylphenols, the... [Pg.229]

The peroxidase-catalyzed polymerization of m-alkyl substituted phenols in aqueous methanol produced soluble phenolic polymers. The mixed ratio of buffer and methanol greatly affected the yields and the molecular weight of the polymer. The enzyme source greatly affected the polymerization pattern of m-substituted monomers. Using SBP catalyst, the polymer yield increased as a function of the bulkiness of the substituent, whereas the opposite tendency was observed when HRP was the catalyst. [Pg.231]

Various bisphenol derivatives were also polymerized by peroxidase under selected reaction conditions, yielding soluble phenolic polymers. Bisphenol-A was polymerized by peroxidase catalyst to give a polymer soluble in acetone, DMF, DMSO, and methanol. The polymer was produced in higher yields using SBP as a catalyst. This polymer showed a molecular weight of 4 x 10 and a 7g at 154°C. The HRP-catalyzed polymerization of 4,4 -biphenol produced a polymer showing high thermal stability. ... [Pg.231]

A bi-enzymatic system (glucose oxidase -I- HRP) was also used to catalyze the synthesis of phenolic polymers. The polymerization of phenol, albeit in moderate yield, was accomplished in the presence of glucose avoiding the addition of hydrogen peroxide (Scheme 2 ), which was formed in situ by the oxidation of glucose catalyzed by glucose oxidase. [Pg.232]

As described above, the enzymatic polymerization of phenols was often carried out in a mixture of a water-miscible organic solvent and a buffer. By adding 2,6-di-0-methyl-(3-cyclodextrin (DM-(3-CD), the enzymatic polymerization of water-insoluble m-substituted phenols proceeded in buffer. The water-soluble complex of the monomer and DM-(3-CD was formed and was polymerized by HRP to give a soluble polymer. In the case of phenol, the polymerization took place in the presence of 2,6-di-O-methyl-a-cyclodextrin (DM-a-CD) in a buffer. Only a catalytic amount of DM-a-CD was necessary to induce the polymerization efficiently. Coniferyl alcohol was oxidatively polymerized in the presence of a-CD in an aqueous solution. ... [Pg.232]

Poly(2,6-dimethyl-l,4-oxyphenylene) (poly(phenylene oxide), PPG) is a material widely used as high-performance engineering plastics, thanks to its excellent chemical and physical properties, e.g., a high 7 (ca. 210°C) and mechanically tough property. PPO was first prepared from 2,6-dimethylphenol monomer using a copper/amine catalyst system. 2,6-Dimethylphenol was also polymerized via HRP catalysis to give a polymer exclusively consisting of 1,4-oxyphenylene unit, while small amounts of Mannich-base and 3,5,3, 5 -tetramethyl-4,4 -diphenoquinone units are always contained in the chemically prepared PPO. [Pg.233]

Laccase (PCL) as well as peroxidases (HRP and SBP) induced a new type of oxidative polymerization of the 4-hydroxybenzoic acid derivatives, 3,5-dimethoxy-4-hydroxybenzoic acid (syringic acid) and 3,5-dimethyl-4-hydroxybenzoic acid. The polymerization involved elimination of carbon dioxide and hydrogen from the monomer to give PPO derivatives with molecular weight up to 1.8 x lO (Scheme 22). - ... [Pg.233]

We prepared a phenol-containing hyaluronan derivative, which was inter-molecularly coupled by HRP to yield a crosslinked hydrogel (Scheme 27). The sequenhal injection of this hyaluronan derivative and peroxidase formed... [Pg.237]

Morphology of the enzymatically synthesized phenolic polymers was controlled under the selected reaction conditions. Monodisperse polymer particles in the sub-micron range were produced by HRP-catalyzed dispersion polymerization of phenol in 1,4-dioxane-phosphate buffer (3 2 v/v) using poly(vinyl methyl ether) as stabihzer. °° ° The particle size could be controlled by the stabilizer concentration and solvent composition. Thermal treatment of these particles afforded uniform carbon particles. The particles could be obtained from various phenol monomers such as m-cresol and p-phenylphenol. [Pg.238]

A new crosslinkable polymer was synthesized by the SBP-catalyzed polymerization of cardanol. When HRP was used as catalyst for the cardanol polymerization, the reaction took place in the presence of a redox mediator (phe-nothiazine derivative) to give the polymer. Fe-salen efficiently catalyzed the polymerization of cardanol in organic solvents (Scheme 29). " The polymerization proceeded in 1,4-dioxane to give the soluble polymer with molecular weight of several thousands in good yields. The curing of the polymer took place in the presence of cobalt naphthenate catalyst at room temperature or thermal treatment (150°C for 30 min) to form yellowish transparent films ( artificial urushi ... [Pg.239]

The HRP-catalyzed polymerization of (-l-)-catechin was carried out in an equivolume mixture of 1,4-dioxane and buffer (pH 7) to give the polymer with molecular weight of 3.0 x 10 in 30% yield. Using methanol as co-solvent improved the polymer yield and molecular weight. In the polymerization of... [Pg.240]

Superoxide anion scavenging activity of the enzymatically synthesized poly(catechin) was evaluated. Poly(catechin), synthesized by HRP catalyst, greatly scavenged superoxide anion in a concentration-dependent manner, and almost completely scavenged at 200 p.M of a catechin unit concentration. The laccase-catalyzed synthesized poly(catechin) also showed excellent antioxidant property. Catechin showed pro-oxidant property in concentrations lower than 300 jlM. These results demonstrated that the enzymatically synthesized poly(catechin) possessed much higher potential for superoxide anion scavenging, compared with intact catechin. [Pg.241]

Mutans streptococci are the major pathogenic organisms of dental caries in humans. The pathogenicity is closely related to production of extracellular, water-insoluble glucans from sucrose by glucosyltransferase and acid release from various fermentable sugars. Poly(catechin) obtained by HRP catalyst in a phosphate buffer (pH 6) markedly inhibited glucosyltransferase from Streptococcus sorbrinus 6715, whereas the inhibitory effect of catechin for this enzyme was very low. [Pg.242]

Polyhedral oligomeric silsesquioxane (POSS) has been extensively studied as starting substrate to construct nanocomposites with precise control of nanoarchitecture and properties. Octahedral derivatives are the most representative ones of this family. It was reported that the HRP-catalyzed conjugation of catechin on amine-substituted octahedral silsesquioxane amplified the beneficial physiological property of flavonoids. The POSS-catechin conjugate exhibited great... [Pg.243]

Single linear developments are mostly employed in the vertical mode. The apph-cabihty of the horizontal mode is discussed in Chapter 6. For circular and anticircular developments, the movement of the mobile phase is two-dimensional however, from the standpoint of sample separation it is a one-dimensional technique. Circular developments result in higher hRp values compared to linear ones imder the same conditions, and compoimds are better resolved in the lower-AR range. The same effect is noticed on plates with a layer thickness gradient (see Section 5.2.1). On the other hand, using antieircular developments, compounds are bettCT resolved in the upper-M range. [Pg.120]

HRA Histamine-releasing activity HRAN Neutrophil-derived histamine-releasing activity HRf Homologous-restriction factor HRF Histamine-releasing factor HRP Horseradish peroxidase HSA Human serum albumin HSP Heat-shock protein HS-PG Heparan sulphate protet ycan... [Pg.283]

R. P. Lcite, G. U. Miinsavage, U. Bonas, and R. E. Stall, Detection and identification of phytopathogenic Xanthomonas species by amplification of DNA-.sequences related to the HRP genes of Xanthomonas-campestris pv. vesicatoria. Appl. Environ. Microbiol. 60 1077 (1994),... [Pg.408]

Jacobs, B.L. Foote, S.L. and Bloom, F.E. Differential projections of neurons within the dorsal raphe nucleus of the rat A horseradish peroxidase (HRP) study. Brain Res 147 149-153, 1978. [Pg.299]

Secondary antibody and determination. A secondary antibody labeled with an enzyme is added which binds to the primary antibody that is bound to the coating antigen. If the primary antibody were produced in a rabbit, an appropriate secondary antibody would be goat anti-rabbit immunoglobulin G (IgG) conjugated with horseradish peroxidase (HRP) (or another enzyme label). Excess secondary antibody is washed away. An appropriate substrate solution is added that will produce a colored or fluorescent product after enzymatic conversion. The amount of enzyme product formed is directly proportional to the amount of first antibody bound to the coating antigen on the plate and is inversely proportional to the amount of analyte in the standards. [Pg.626]

De Olmos J.S., Hardy H. and Heimer L. (1978). The afferent connections in the main and accessory olfactory bulb formations in the rat an experimental HRP study. J Comp Neurol 181, 213-244. [Pg.200]


See other pages where HRP is mentioned: [Pg.268]    [Pg.105]    [Pg.415]    [Pg.21]    [Pg.456]    [Pg.228]    [Pg.228]    [Pg.230]    [Pg.231]    [Pg.233]    [Pg.234]    [Pg.235]    [Pg.235]    [Pg.236]    [Pg.771]    [Pg.69]    [Pg.128]    [Pg.430]    [Pg.431]    [Pg.431]    [Pg.431]    [Pg.432]    [Pg.11]   
See also in sourсe #XX -- [ Pg.3 , Pg.4 , Pg.9 , Pg.11 , Pg.12 , Pg.18 , Pg.21 , Pg.23 , Pg.160 , Pg.187 , Pg.212 , Pg.214 , Pg.215 , Pg.221 , Pg.222 , Pg.236 , Pg.314 , Pg.319 , Pg.321 , Pg.325 , Pg.338 ]




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Affinity Purification of HRP

Assays with HRP

Avidin HRP conjugate

Avidin HRP using reductive

Chemiluminescence Using HRP

Detection Using Horseradish Peroxidase (HRP)

Didodecyldimethylammonium bromide HRP immobilization

Direct electron transfer of HRP

HRP compound

HRP immobilization

HRP-catalyzed oxidation

HRP-catalyzed oxidation of phenols

Horseradish peroxidase, HRP

Indirect EIA with HRP Conjugate

Inhibition of HRP

Labeled HRP

Periodate oxidation of HRP

Periodate-Oxidized HRP to Antibodies by Reductive Amination

Recombinant HRP

Recombinant HRP isoenzyme

Streptavidin HRP using reductive

Streptavidin-HRP

Sulfo-SMCC HRP with

Synthesis of PANI Using Enzymes Different From HRP

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