Results 181 to 190 of about 16,901 (208)
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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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Functional attachment of horse radish peroxidase to plasma-treated surfaces
SPIE Proceedings, 2004Controlling the interaction of surfaces with macromolecules, such as proteins and antibodies, is the key to producing biocompatible prosthetic devices, biosensors and diagnostic arrays. The development of technologies to control these interactions will result in the early detection of disease and have the potential to dramatically reduce costs ...
Marcela M. Bilek +7 more
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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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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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Journal of Immunological Methods, 1983
A simple and sensitive method for measurement of the release of H2O2 from phagocytic cells is described. The assay is based on the H2O2-dependent oxidation of homovanillic acid (3-methoxy-4-hydroxyphenylacetic acid, HVA) to a highly fluorescent dimer (2,2'-dihydroxy-3,3'-dimethoxydiphenyl-5,5'-diacetic acid) which is mediated by horse-radish peroxidase.
W, Ruch, P H, Cooper, M, Baggiolini
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A simple and sensitive method for measurement of the release of H2O2 from phagocytic cells is described. The assay is based on the H2O2-dependent oxidation of homovanillic acid (3-methoxy-4-hydroxyphenylacetic acid, HVA) to a highly fluorescent dimer (2,2'-dihydroxy-3,3'-dimethoxydiphenyl-5,5'-diacetic acid) which is mediated by horse-radish peroxidase.
W, Ruch, P H, Cooper, M, Baggiolini
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Absorption of horse-radish peroxidase by the mucosal cells of the duodenum of mouse
Histochemie, 1971Horse-radish peroxidase was injected intraperitonealy to fasted and fed newborns. The protein was rapidly absorbed by the fasting animals and more slowly by the fed newborns. The tracer was progressively segregated into the supranuclear cluster of dense tubules and dense bodies.
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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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Pseudo-catalatic mode of horse radish peroxidase
Free Radical Biology and Medicine, 1998openaire +1 more source