Structural homology between mouse liver and horse spleen ferritins
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چکیده
منابع مشابه
Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase.
The three-dimensional structure of a ternary complex of horse liver alcohol dehydrogenase with reduced nicotinamide adenine dinucleotide and the inhibitor dimethyl sulfoxide has been determined to 4.5 A resolution independently of the apoenzyme structure. The electron density maps of both structures have been compared. The two coenzyme binding domains which form the center of the dimer molecula...
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Antigenic relationship between purified equine infectious anemia (EIA) virus and spleen-derived antigen from EIA-infected horses was examined by immunodiffusion. Identical antigenicity of these two antigens has been proven because precipitation lines formed between the two antigens and EIA antiserum connected with each other. The results indicate that the antigenic substance derived from infect...
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Background: The present study was designed to evaluate the homing potential of mouse embryonic stem cells (ESC) treated with erythropoietin (EPO) in hematopoietic organs such as spleen and liver after transplantation using morphological and immuno-histochemical techniques. Methods: Day-four embryoid body (EB)-derived cells were dissociated and re-plated in medium in the presence and absence of ...
متن کاملHeterogeneity in tissue ferritins displayed by gel electrofocusing.
1. Horse spleen ferritin and human liver ferritin were examined by gel electrofocusing under conditions that demonstrated equilibrium focusing. Both ferritins were resolved into multiple isoferritins. Both families of isoferritins were separable from one another. 2. Horse spleen ferritin was also resolved into five components by ion-exchange chromatography on DEAE-Sephadex A-50. Each of the maj...
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...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)81135-2