Results 241 to 250 of about 531,624 (298)
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Photochemistry and Photobiology, 1981
— Inactivation of catalase with visible light (>400nm) has been studied in purified bovine liver catalase and in peroxisomal catalase in the mitochondrial fraction of rat liver. Light corresponding to that of maximal absorbance of the heme site (405 nm) was most effective in inactivation.
L, Cheng, E W, Kellogg, L, Packer
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— Inactivation of catalase with visible light (>400nm) has been studied in purified bovine liver catalase and in peroxisomal catalase in the mitochondrial fraction of rat liver. Light corresponding to that of maximal absorbance of the heme site (405 nm) was most effective in inactivation.
L, Cheng, E W, Kellogg, L, Packer
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Current Protocols in Toxicology, 2006
AbstractCatalase (hydrogen peroxide/hydrogen peroxide oxidoreductase) is an important cellular antioxidant enzyme that defends against oxidative stress. It is found in the peroxisomes of most aerobic cells. It serves to protect the cell from toxic effects of high concentrations of hydrogen peroxide (H2O2) by catalyzing its decomposition into molecular ...
Nandita, Shangari, Peter J, O'Brien
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AbstractCatalase (hydrogen peroxide/hydrogen peroxide oxidoreductase) is an important cellular antioxidant enzyme that defends against oxidative stress. It is found in the peroxisomes of most aerobic cells. It serves to protect the cell from toxic effects of high concentrations of hydrogen peroxide (H2O2) by catalyzing its decomposition into molecular ...
Nandita, Shangari, Peter J, O'Brien
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Biochemical Genetics, 1970
An examination of three inbred strains of mice differing with respect to liver and kidney catalase activity reveals two distinct genetic factors controlling the level of liver catalase activity. The first genetic factor controls the catalytic activity of the enzyme.
Ganschow, R E, Schimke, R T
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An examination of three inbred strains of mice differing with respect to liver and kidney catalase activity reveals two distinct genetic factors controlling the level of liver catalase activity. The first genetic factor controls the catalytic activity of the enzyme.
Ganschow, R E, Schimke, R T
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Journal of Integrative Plant Biology, 2018
Hydrogen peroxide (H2 O2 ) is generated in many metabolic processes. As a signaling molecule, H2 O2 plays important roles in plant growth and development, as well as environmental stress response.
Tong Su +12 more
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Hydrogen peroxide (H2 O2 ) is generated in many metabolic processes. As a signaling molecule, H2 O2 plays important roles in plant growth and development, as well as environmental stress response.
Tong Su +12 more
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2000
Abstract The enzyme catalase, widely distributed in animal tissues, consists of four identical subunits. The molecular weight is approximately 240000. The major active component of the enzyme, ferri protoporphyrin (haematin).
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Abstract The enzyme catalase, widely distributed in animal tissues, consists of four identical subunits. The molecular weight is approximately 240000. The major active component of the enzyme, ferri protoporphyrin (haematin).
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Electron Transfer in Catalases and Catalase-Peroxidases
2013Catalases (EC 1.11.1.6) are enzymes that catalyze the disproportionation of hydrogen peroxide into water and molecular oxygen by means of a heme iron or a dimanganese active site. They are crucial metalloproteins regulating the cellular concentration of hydrogen peroxide, which has a concentration-dependent dual role in cell signaling and oxidative ...
Ivancich, Anabella, Loewen, Peter C.
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Science, 1965
The enzymatic activity of catalase is lost during exposure to sunlight in the presence of oxygen. A simultaneous decline occurs in the absorption peak at 405 nanometers.
R. L. Mitchell, I. C. Anderson
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The enzymatic activity of catalase is lost during exposure to sunlight in the presence of oxygen. A simultaneous decline occurs in the absorption peak at 405 nanometers.
R. L. Mitchell, I. C. Anderson
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Colorimetric assay of catalase.
Analytical Biochemistry, 1972A. Sinha
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