Results 251 to 260 of about 358,018 (300)

Chromogenic substrates for horseradish peroxidase

Analytical Biochemistry, 1991
Two new detection systems for horseradish peroxidase (HRP) have been developed for the staining of membranes used in immunoassays. These systems use dimethyl or diethyl analogues of p-phenylenediamine with 4-chloro-1-naphthol to generate a blue product or 3-methyl-2-benzothiazolinone hydrazone with 4-chloro-1-naphthol to generate a red product.
S M, Conyers, D A, Kidwell
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Preparation of Horseradish Peroxidase-Labeled Probes

Molecular Biotechnology, 1996
The direct labeling of nucleic acid probes with horseradish peroxidase (HRP) may be used in many membrane hybridization applications, including Southern blots, Northern blots, colony and plaque screening, PCR products detection/identification. This article describes the preparation method, which involves the labeling of a single-stranded nucleic acid ...
I, Durrant, T, Stone
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The oxidation of horseradish peroxidase by periodate

Biochemical and Biophysical Research Communications, 1968
Abstract A chemical mechanism for the action of horseradish peroxidase (HRP) has been proposed recently (Brill and Weinryb, 1967) . One of the features of this mechanism is the association of an oxidizing equivalent with a methine bridge carbon atom in Compound I, in accord with earlier suggestions by Chance (1949) and Brill and Williams (1961) .
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Oxidative Degradation of Alkylphenols by Horseradish Peroxidase

Journal of Bioscience and Bioengineering, 2003
Alkylphenols such as bisphenol A (2,2-bis(4-hydroxyphenyl)propane; BPA), p-nonylphenol (p-NP), and p-octylphenol (p-OP) that are known as endocrine disrupters were oxidized by horseradish (Armoracia rusticana) peroxidase (HRP) with H2O2. The optimal pHs for BPA, p-NP, and p-OP were 8.0, 7.0, and 5.0, respectively. The optimal temperature for BPA was 20
Hisae, Sakuyama, Yasushi, Endo, Kenshiro, Fujimoto, Yasuhiko, Hatana   +3 more
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Hydroxylation of benzene by horseradish peroxidase and immobilized horseradish peroxidase in an organic solvent

Bioorganic & Medicinal Chemistry Letters, 1995
Abstract Horseradish peroxidase (HRP) catalyzed hydroxylation of benzene with an oxidant when benzene was used as the reaction solvent. HRP immobilized on poly(γ-methyl-L-glutamate) also catalyzed the reaction with higher activity than that of free HRP.
Reiko Akasaka, Tadahiko Mashino, Masaaki Hirobe   +2 more
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Horseradish peroxidase. XXXVI. On the difference between peroxidase and metmyoglobin

Biochemical and Biophysical Research Communications, 1979
Abstract A mechanism for the reaction of hydrogen peroxide with horseradish peroxidase is proposed which involves the catalytic activity of the carboxylate side chain of aspartate residue 43. The corresponding residue in the active site of metmyoglobin is glycine E8, which explains the inability of metmyoglobin to form compound I.
H B, Dunford, T, Araiso
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Alkylation of horseradish peroxidase with lodoacetate

Archives of Biochemistry and Biophysics, 1968
Abstract A kinetic and chemical study of the inactivation of horseradish peroxidase by reaction with iodoacetate has been undertaken to gain insight into the chemical behavior and reactivity of the protein moiety with a view toward fully defining the catalytic site of the enzyme.
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Metabolism of 3,3′ -dichlorobenzidine by horseradish peroxidase

Xenobiotica, 1988
1. The peroxidatic oxidation of 3,3'-dichlorobenzidine by horseradish peroxidase in the presence of H2O2 was examined spectrophotometrically and the reactivity of the spectral species were compared to those formed from the peroxidative oxidation of benzidine. 2.
B, Lang, M M, Iba
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Conjugation of Antibodies to Horseradish Peroxidase

2005
Horseradish peroxidase is coupled to IgG antibody in a two-step procedure. In the first step monosaccharide residues in the enzyme are oxidized with periodate to produce aldehyde groups. Then, in the second step, the aldehyde groups are allowed to react with amino groups in the IgG antibody.
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OXYGEN DIFFUSION THROUGH HORSERADISH PEROXIDASE

Photochemistry and Photobiology, 1990
Abstract— The quenching by molecular oxygen of the fluorescence from a protoporphyrin IX adduct of horseradish peroxidase has been investigated using both intensity and time‐resolved techniques. The bimolecular quenching rate constant determined for this process, as evaluated by the conventional Stern‐Volmer analysis, was 2 × 108 M−1 s−1, among the ...
J E, Brunet, C, Jullian, D M, Jameson
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