Results 181 to 190 of about 33,656 (216)
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Substratum specificity of purified peroxidase isoenzymes of horse radish root
Experientia, 1973An sieben aus Meerrettichwurzeln isolierten Isoenzymen der Peroxydase konnte substratspezifisches Verhalten nachgewiesen werden.
Dana Iordăchescu +2 more
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Dissociation into subunits of thyroglobulin iodinated by thyroid and horse radish peroxidase
Biochimie, 1973Summary Several sheep thyroglobulin samples were prepared containing different and increasing amounts of iodine. The iodination of these preparations was performed using either thyroid peroxidase (TPO) or horse radish peroxidase (HRP). Each thyroglobulin preparation was dissociated into 12 S subunits by sodium dodecyl sulfate treatment and the ...
J, Pommier, D, Deme, J, Nunez
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Absorption of horse-radish peroxidase by the conjunctival epithelium of monkeys and rabbits
Graefes Archive for Clinical and Experimental Ophthalmology, 1983Horse-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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Fluid flow in the liver demonstrated with horse radish peroxidase
American Journal of Anatomy, 1968AbstractUsing horse radish peroxidase as a tracer for fluid flow, rapid diffusion was demonstrated between sinusoidal lumina and the interhepatocytic spaces of the murine liver. The marker passed rapidly between adjacent sinusoidal cells and filled the space of Disse. Appreciable amounts of peroxidase were also seen in pinocytic and phagocytic vacuoles
J M, Papadimitriou, M N, Walters
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The Immobilization of Horse Radish Peroxidase on a Metal Surface
1991Chemical 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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Analytica Chimica Acta, 1979
Abstract An enthalpimetric method is described for the determination of peroxidase activity based on the heat produced by the peroxidase-catalysed oxidation of iodide by hydrogen peroxide. Two other electron donors, hydroquinone and ascorbic acid, were found to be less suitable as substrates.
J. Keith Grime, Kenneth R. Lockhart
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Abstract An enthalpimetric method is described for the determination of peroxidase activity based on the heat produced by the peroxidase-catalysed oxidation of iodide by hydrogen peroxide. Two other electron donors, hydroquinone and ascorbic acid, were found to be less suitable as substrates.
J. Keith Grime, Kenneth R. Lockhart
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A Kinetic Study of the Horse-Radish Peroxidase-Catalyzed Oxidation of Iodide
European Journal of Biochemistry, 1968Reaction 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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Isoelectric Properties of Gamma-irradiated Horse-radish Peroxidase
International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1971Delincee, H., Radola, B. J., Drawert, F.
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The uptake of injected horse‐radish peroxidase by lysosome‐rich histiocytes
The Journal of Pathology and Bacteriology, 1968J F, Kerr, G, Middleton
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The Kinetics of Fluoride Binding by Ferric Horse Radish Peroxidase*
Biochemistry, 1967H B, Dunford, R A, Alberty
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