Results 251 to 260 of about 270,169 (306)
Ice-Cold Temperature Enhances NADPH Oxidase-Dependent Release of Tissue Factor-Bearing Extracellular Vesicles from Human Monocytic Cells. [PDF]
Life (Basel)Nishioka A, Azma T, Mieda T, Mio Y.
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ENCAPSULATION OF CATALASE AND PEG-CATALASE IN ERYTHROCYTE [PDF]
Artificial Cells, Blood Substitutes, and Biotechnology, 2001 Reactive partially reduced oxygen species such as superoxide anion (O2-), hydrogen peroxide (H2O2) and hydroxyl radical (OH) are produced in aerobically growing organisms during normal cellular respiration. To provide an effective defense against these reactive species, many aerobic organisms have evolved a multienzyme defense which includes superoxide
Baysal, SH, Uslan, AH
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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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Immobilization of catalase on chitosan film [PDF]
Enzyme and Microbial Technology, 2000 Catalase was immobilized on the chitosan film that is a natural polymer. Studies were done on free catalase and immobilized catalase on chitosan film concerning the determination of optimum temperature, optimum pH, thermal stability, storage stability ...
Senay Akkuş Cetinus
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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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Journal of Molecular Biology, 1985
The refined structure of beef liver catalase (I. Fita, A. M. Silva, M. R. N. Murthy & M. G. Rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms. The distal side of the deeply buried heme pocket is connected with the surface of the molecule by one (or possibly two) channel.
I, Fita, M G, Rossmann
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The refined structure of beef liver catalase (I. Fita, A. M. Silva, M. R. N. Murthy & M. G. Rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms. The distal side of the deeply buried heme pocket is connected with the surface of the molecule by one (or possibly two) channel.
I, Fita, M G, Rossmann
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Progress in Biophysics and Molecular Biology, 2018
Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics.
Hessam, Sepasi Tehrani +1 more
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Catalase is one of the firsts in every realm of biological sciences. At the same time it also has a number of unusual features. It has one of the highest turnover numbers of all enzymes. It is essential for neutralizing the noxious hydrogen peroxide both in the nature and the various industries such as dairy, textile and pharmaceutics.
Hessam, Sepasi Tehrani +1 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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