3P075 Insertion of ferroxidase center in horse L ferritin subunit(01D. Protein: Function,Poster)
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چکیده
منابع مشابه
Construction of a ferroxidase center in human ferritin L-chain.
Ferritins are 24-mer proteins which store and detoxify intracellular iron. Mammalian ferritins are made of two subunit types, the H- and L-chains, with different functional specificity. The H-chain has a metal-binding site (the ferroxidase center) which confers ferroxidase activity to the protein and accelerates iron incorporation. In the L-chain the center is substituted by a salt bridge. We p...
متن کاملFerroxidase kinetics of horse spleen apoferritin.
Protein ferroxidase site(s), which catalyze the reaction between ferrous ion and dioxygen, have long been thought to play a role in core formation in ferritin; however, the mechanism of the reaction has never been studied in detail. In the present work, the enzymatic activity of ferritin was examined using oximetry, the net Fe2+ oxidation reaction being as follows. [formula: see text] The react...
متن کاملIncorporation and release of inorganic phosphate in horse spleen ferritin.
When ferritin is reconstituted from Fe and apoferritin in vitro in the presence of Pi, the product obtained differs both from native ferritin and from ferritin reconstituted in the absence of Pi. When the latter is incubated with Pi the product resembles native ferritin with respect both to the pattern of Pi incorporated per molecule or per Fe atom and to the ease of release of this Pi relative...
متن کاملFerritin stimulation of a monokine inhibitor of lipopolysaccharide-augmented myelopoiesis is ferroxidase dependent.
Ferritin inhibition of myelopoiesis has been associated with intrinsic ferroxidase activity of heavy-chain ferritin and with production of a monokine inhibitor of lipopolysaccharide (LPS)-augmented monocytopoiesis. We report here that intrinsic ferroxidase activity of heavy-chain ferritin is required for stimulated production of the monokine inhibitor of LPS-augmented monocytopoiesis.
متن کاملSynthesis and interfacing of biocompatible iron oxide nanoparticles through the ferroxidase activity of Helicobacter Pylori ferritin.
Ferritin is an iron storage protein that is often used to coat metallic nanoparticles, such as iron oxide nanoparticles (IONPs). However, the synthesis and biocompatibility of ferritin-coated IONPs remain unclear. Therefore, this study reports the synthesis of a ferritin gene cloned and expressed from Helicobacter pylori (HPFn). The ferroxidase activity of the synthase HPFn was used for the de ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2013
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.53.s224_3