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Molecular and Cellular Biochemistry, 1988 It is well known that the partial reduction of oxygen can result in the formation of highly reactive oxygen products. Hydrogen peroxide is one of these metabolites of oxygen. Peroxidases utilize this metabolite for a variety of functions. It is the purpose of this treatise to review the nature and function of various membrane peroxidases in the body.
Banerjee, Ranajit K.
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Oscillations in the peroxidase-oxidase reaction: a comparison of different peroxidases
Biochimica et Biophysica Acta (BBA) - General Subjects, 1996 The nonlinear behavior of the peroxidase-oxidase reaction was studied using structurally different peroxidases. For the first time sustained oscillations with peroxidases other than horseradish peroxidase in a single-enzyme system were observed. All peroxidases that showed significant oxidase activity were able to generate sustained oscillations.
Kummer, Ursula +4 more
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2013 With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
Brigelius Flohé R, MAIORINO, MATILDE
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Redox properties of heme peroxidases
Archives of Biochemistry and Biophysics, 2010 Peroxidases are heme enzymes found in bacteria, fungi, plants and animals, which exploit the reduction 24of hydrogen peroxide to catalyze a number of oxidative reactions, involving a wide variety of organic and 25inorganic substrates. The catalytic cycle
Gianantonio Battistuzzi +2 more
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Neurodegeneration and peroxidases
Neurobiology of Aging, 2009Alzheimer's disease (AD), Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS) are neurodegenerative diseases that affect different parts of the central nervous system. However, a review of the literature indicates that certain biochemical reactions involved in neurodegeneration in these three diseases are quite similar and could be partly ...
Johannes, Everse, Penelope W, Coates
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Peroxidases of Trypanosomatids
Antioxidants & Redox Signaling, 2008This article provides an overview about the recent advances in the dissection of the peroxide metabolism of Trypanosomatidae. This family of protozoan organisms comprises the medically relevant parasites Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp.
Helena, Castro, Ana M, Tomás
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Molecular and Cellular Biochemistry, 1986
Peroxidases are known to be involved in the intracellular metabolism of H2O2 coupled with various physiological functions. Apart from the thyroid gland, the enzyme has been isolated from various extrathyroidal sources of which salivary gland is one of the richest sources of the enzyme.
R K, Banerjee, A G, Datta
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Peroxidases are known to be involved in the intracellular metabolism of H2O2 coupled with various physiological functions. Apart from the thyroid gland, the enzyme has been isolated from various extrathyroidal sources of which salivary gland is one of the richest sources of the enzyme.
R K, Banerjee, A G, Datta
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Chemico-Biological Interactions, 2000
The family of human peroxidases described includes myeloperoxidase, eosinophil peroxidase, uterine peroxidase, lactoperoxidase, salivary peroxidase, thyroid peroxidase and prostaglandin H1/2 synthases. The chemical identity of the peroxidase compound I and II oxidation states for the different peroxidases are compared.
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The family of human peroxidases described includes myeloperoxidase, eosinophil peroxidase, uterine peroxidase, lactoperoxidase, salivary peroxidase, thyroid peroxidase and prostaglandin H1/2 synthases. The chemical identity of the peroxidase compound I and II oxidation states for the different peroxidases are compared.
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Common phylogeny of catalase-peroxidases and ascorbate peroxidases
Gene, 2000Catalase-peroxidases belong to Class I of the plant, fungal, bacterial peroxidase superfamily, together with yeast cytochrome c peroxidase and ascorbate peroxidases. Obviously these bifunctional enzymes arose via gene duplication of an ancestral hydroperoxidase. A 230-residues long homologous region exists in all eukaryotic members of Class I, which is
M, Zámocký, S, Janecek, F, Koller
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Current Opinion in Biotechnology, 1993
The availability of recombinant cytochrome c peroxidase from yeast has already proved to be of considerable importance in developing the protein engineering of peroxidases and of metalloproteins in general. With the recent increase in information on peroxidase sequences, further developments in recombinant expression systems and the determination of an
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The availability of recombinant cytochrome c peroxidase from yeast has already proved to be of considerable importance in developing the protein engineering of peroxidases and of metalloproteins in general. With the recent increase in information on peroxidase sequences, further developments in recombinant expression systems and the determination of an
openaire +2 more sources