Amino acid sequence of horse spleen apoferritin
                    
                        
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                    چکیده
منابع مشابه
Ferroxidase 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 کاملHydrogen ion interactions of horse spleen ferritin and apoferritin.
The interactions of horse spleen ferritin and its derivative apoferritin with H+ ions were studied by potentiometric and spectrophotometric titration; to aid in data analysis, heats of ionization over a limited pH range and amide content were also determined. Per apoferritin subunit, all tyrosine and cysteine side chains, two of the nine lysine side chains and at least three of the six histidin...
متن کاملAmino acid sequence of porcine spleen cathepsin D.
The amino acid sequence of porcine spleen cathepsin D heavy chain has been determined and, hence, the complete structure of this enzyme is now known. The sequence of heavy chain was constructed by aligning the structures of peptides generated by cyanogen bromide, trypsin, and endo-proteinase Lys C cleavages. The structure of the light chain has been published previously. The cathepsin D molecul...
متن کاملInitial iron oxidation in horse spleen apoferritin. Characterization of a mixed-valence iron(II)-iron(III) complex.
In ferritin, iron is stored by oxidative deposition of the ferrous ion to form a hydrous ferric oxide mineral core. Two intermediates, formed during the initial stages of iron accumulation in apoferritin, have been observed previously in our laboratory and have been identified as a mononuclear Fe3(+)-protein complex and a mixed-valence Fe2(+)-Fe3(+)-protein complex. The physical characteristics...
متن کاملAmino acid sequence of copper-zinc superoxide dismutase from horse liver.
The complete amino acid sequence of copper-zinc superoxide dismutase from horse liver is reported. The molecule consists of 153 amino acids and has a Mr = 16,000. The primary structure was determined by automated and manual sequence analysis on fragments produced by cleavage of the S-carboxymethylated protein with cyanogen bromide and on peptides obtained by digestion with trypsin, thermolysin,...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1981
ISSN: 0014-5793
DOI: 10.1016/0014-5793(81)80193-7