Results 221 to 230 of about 211,060 (265)
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ENCAPSULATION OF CATALASE AND PEG-CATALASE IN ERYTHROCYTE
Artificial Cells, Blood Substitutes, and Biotechnology, 2001Reactive 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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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The refined structure of beef liver catalase (I. Fita, A. M. Silva, M. R. N. Murthy & M. G. Rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms.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The refined structure of beef liver catalase (I. Fita, A. M. Silva, M. R. N. Murthy & M. G. Rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms.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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Catalases—With and Without Heme
1988Catalases (H2O2:H2O2 oxidoreductase; EC 1.11.1.6) are metalloenzymes that catalyze the elimination of H2O2 according to the equation: Open image in new window Catalases, together with superoxide dismutases and peroxidases, provide aerobic cells with a defense system for removal of superoxide radical and of hydroperoxides.
W F, Beyer, I, Fridovich
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Catalase in Insect Trypanosomatids*
The Journal of Protozoology, 1963SYNOPSIS. Seven monoxenous Trypanosomatidae, Crithidia fasciculata (Anopheles strain), C. fasciculata (Culex pipiens, Wallace), C. fasciculata (Culex pipiens, Nöller), C. luciliae, C. sp. from Euryophthalmus, “Strigomonas” oncopelti and Blastocrithidia culicis all are catalase‐positive. S. oncopelti is only catalase‐positive when grown in hemin‐media.
D M, WERTLIEB, H N, GUTTMAN
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Insensitivity of erythrocyte catalase to substances that depress liver catalase
Experientia, 1961La tirosina che inibiscein vivo l'attivita della catalasi epatica dei topi edin vitro l'attivita della catalasi cristallizzata, ed una frazione di albumine denaturate attiva sulla catalasi soloin vivo, si sono dimostrate inattive sulla catalasi eritrocitaria.
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