Results 171 to 180 of about 16,901 (208)
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The oxidation of naphthalene sulfonate dyes by horse radish peroxidase

Archives of Biochemistry and Biophysics, 1982
Abstract Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10 −12 m concentrations of the enzyme and permits determination of very low levels of peroxides.
L, Sasson, M, Sharabani, I, Aviram
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Degratation of 3-hydroxyflavone by horse radish peroxidase

Biochemical and Biophysical Research Communications, 1975
Abstract A hydroxylic group in position 3 and a double bond between positions 2 and 3 is the minimum requirement for flavones to be substrates for horse radish peroxidase (EC 1.11.1.7). 3-Hydroxyflavone, fulfilling these requirements, yields on enzymatic cleavage salicylic, phenylglyoxylic and probably benzoic acid.
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Inhibition of horse radish peroxidase by specific antisera

Molecular Immunology, 1973
Abstract Antiperoxidase has been prepared in the rabbit, cat, mouse, hamster and chicken. All of these antisera inhibit peroxidase activity.
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Absorption of horse-radish peroxidase by the conjunctival epithelium of monkeys and rabbits

Graefes Archive for Clinical and Experimental Ophthalmology, 1983
Horse-radish peroxidase was instilled into the conjunctival sac of rabbits and Cynomolgus monkeys. After an interval of 5, 30 or 60 min the conjunctival epithelium was studied by electron microscopy. The tracer was found to be absorbed predominantly by type-V cells, which are rich in mitochondria; this process was found to occur more rapidly in the ...
P, Steuhl, J W, Rohen
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Production of horse radish peroxidase by plant cell culture

Journal of Chemical Technology & Biotechnology, 1987
AbstractCalluses were induced from the stem and the root tissues of horse radish plantlets. Cell aggregate selections were carried out on them to obtain a cell line with higher peroxidase activity, and the isozyme patterns of the peroxidases from the cultured cells and their utility values as a clinical diagnostic reagent were investigated.The ...
Yasuyuki Yamada   +5 more
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The Immobilization of Horse Radish Peroxidase on a Metal Surface

1991
Chemical modification of aluminum and copper surfaces and the adsorption of peroxidase (HRPO E.C. 1.11.1.7) onto these surfaces have been investigated using Fourier Transform Infrared Spectroscopy (FT-IR). The pretreatment of an aluminum surface with titanium tetrachloride increases the activity of adsorbed peroxidase by a factor of 7.
V. I. Silin, V.-R. Taliené, A. Tamulis
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Oxidation of homogentisic acid catalyzed by horse-radish peroxidase

Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
Horse-radish peroxidase catalyzes the oxidation of homogentisic acid in the presence of sulfhydryl compounds to form products similar to those obtained by the spontaneous reaction of benzoquinoneacetic acid with sulfhydryl agents. Other heme proteins, such as catalase, cytochrome c, hemoglobin and methemoglobin, do not catalyze this oxidation.
B LADU, V ZANNONI
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Changes in catalytic activity of conjugated horse-radish peroxidase

1986
To investigate how different sizes of protein ligands change peroxidase catalytic activity, we labeled IgG and chorionic somatommamotropin (HCS) with horse radish peroxidase (HRP) by two-step glutaraldehyde method. Guiacol and o-phenylendiamidine (OPD) were used as hydrogen donors.
Malnar, Miljenko   +3 more
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A Kinetic Study of the Horse-Radish Peroxidase-Catalyzed Oxidation of Iodide

European Journal of Biochemistry, 1968
Reaction steps in which H+ and I− are added to horse-radish peroxidase have been studied by examining the steady-state kinetics of the peroxidase-catalyzed oxidation of I−. For this purpose spectrophotometric methods for following the reaction were developed.
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