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2 edition of Spectroscopic studies on apoferritin. found in the catalog.

Spectroscopic studies on apoferritin.

Elizabeth Godbehere

Spectroscopic studies on apoferritin.

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Published .
Written in English


Edition Notes

Thesis (Ph.D.) - University of Sheffield, Department of Chemistry, 1984.

ID Numbers
Open LibraryOL13956449M

We performed reproducible atomic resolution Transmission Electron Microscopy and Wide Angle X-ray Scanning Microscopy experiments studying for the first time the nanoscale properties of a pristine fiber taken from the Turin Shroud. We found evidence of biologic nanoparticles of creatinine bounded with small nanoparticles of iron oxide. The kind, size and distribution of the iron oxide Cited by: 1. Apoferritin as an ubiquitous nanocarrier with excellent shelf life Simona Dostalova,1,2 Katerina Vasickova,1 David Hynek,1,2 Sona Krizkova,1,2 Lukas Richtera,1,2 Marketa Vaculovicova,1,2 Tomas Eckschlager,3 Marie Stiborova,4 Zbynek Heger,1,2 Vojtech Adam1,2 1Department of Chemistry and Biochemistry, Mendel University in Brno, 2Central European Institute of Technology, Brno University Cited by: 7.


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Spectroscopic studies on apoferritin. by Elizabeth Godbehere Download PDF EPUB FB2

Spectroscopic Studies on the Binding of Iron, Terbium, and Zinc by Apoferritin Amyra Treffry and Pauline M. Harrison Department of Biochemistry, The University, Sheffield, U.K. ABSTRACT Ultraviolet difference spectroscopy has been used to study Fe (II11`apoferritin complexes formed after addition of Cited by: Earlier crystallographic and spectroscopic studies had shown that horse spleen apoferritin was capable of removing the metal ion from hemin (Fe(III)-protoporphyrin IX) [G.

Précigoux, J. Yariv, B. A combined spectroscopic methodology of circular dichroism (CD), magnetic CD (MCD), and variable-temperature, variable-field (VTVH) MCD has been applied to define the wild-type (WT) substrate site in M ferritin under biologically relevant solution conditions, 24 enabling its comparison to the binuclear non-heme iron cofactor sites.

8−10,24 CD and MCD spectroscopies probe the ligand-field Cited by: 5. Apoferritin from horse spleen was the first protein cage studied and used as a template for the synthesis of inorganic nanoparticles.

Apoferritin has found extensive use in the synthesis of numerous metallic nanoparticles including Pd 2+, Cu 2+, Fe 2+, Co 2+, Cr 3+, Ni 2+, Mn 2+, Cd 2+, and Zn 2+. Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals.

In humans, it acts as a buffer against iron deficiency and iron overload. Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the InterPro: IPR The complete amino acid sequence of human spleen apoferritin has been determined. and spectroscopic studies of ferritin led to the proposal that the oxidation/translocation path involves a.

Mössbauer spectroscopic and magnetic measurements have been made on a novel magnetic protein produced by the controlled reconstitution of ferritin.

The data indicate that the predominant mineral form in the iron-containing cores is maghemite (γ Cited by: Gel Filtration Markers Kit for Protein Molecular Weig, Da.

1 Product Result. Apoferritin is a gel filtration molecular weight marker that can be used in gel filtration chromatography and protein chromatography. Apoferritin has the ability to demetallate hemin and to metallate protoporphyrin IX. Apoferritin from equine spleen.

The approximate molecular weight of this product isWhat is the concentration of. Apoferritin from horse spleen can be reversibly dissociated at pH 2 or in M G-HCl (pH ).

Reconstitution of the native icositetramer in M TEA buffer (pH ) in the presence of 1 mM EDTA and 3 mM dithioerythritol leads to yields higher than 80%. To monitor the kinetic mechanism, intrinsic fluorescence, far-UV circular dichroism, and covalent cross-linking with glutaraldehyde were Cited by: Previous studies showed that schistosomiasis and malaria and are the main risk factors for anemia in young adults13 % of pupils in group I and 96% of group II students said ferritin as a storage form of iron, while students in both groups used apoferritin as a storage form.

Ferritin and apoferritin (l-3) from horse spleen were made available to the writer by Dr. Michaelis and Dr. Granick of The Rockefeller Institut>e for Medical Research.

Roth crystallize in isotropic octahedra. The individual crystals were too small for single crystal x-ray studies but be. (2, 3), although recent studies suggest that some variation in subunit constitution may be present (4). Relatively little is known about the primary structure or conformation of the subunits.

A high LY helix content is known to be present (2, 5) and a few side chain modification studies have been reported (). apoferritin: [ ap″o-fer´ĭ-tin ] an apoprotein that can bind many atoms of iron per molecule to form ferritin, the form in which iron is stored in the liver and other tissues.

Abbreviations. EPR, electron paramagnetic resonance. MMO, methane monooxygenase. PfFtn, Pyrococcus furiosus ferritin. RNR, ribonucleotide reductase. SVD, singular value decomposition.

A di‐iron catalytic center is key to the functioning of ferritin, the ubiquitous iron‐storage protein of life [].Unlike the di‐iron cofactor site in dioxygen‐activating enzymes, the di‐iron center Cited by: 4. Apoferritin definition, a homogeneous protein, found especially in the intestinal mucosa and the liver, that interacts with a ferric hydroxide-ferric phosphate complex to form ferritin.

See more. Protein immobilization is imperative for bioengineering and biochemical applications. Although many excellent approaches have been proposed, most require elaborate skills and labor-intensive techniques. In this work, we report that phenothiazine compounds such as thionine chloride (TC) are potential molecular adhesives for protein by: nm nanoceria particles are successfully encapsulated into the apoferritin cavity via a dissociation–reconstruction route.

The apoferritin coating not only improves the biocompatibility and changes the cellular uptake route of nanoceria, but also manipulates the Cited by:   The iron storage protein ferritin consists of a spherical polypeptide shell (apoferritin) surrounding a 6-nanometer inorganic core of the hydrated iron oxide ferrihydrite (5Fe2OH2O).

Previous studies have shown that the in vitro reconstitution of apoferritin yields mineral cores essentially identical to those of the native proteins. A magnetic mineral was synthesized within the Cited by: Clark, P.E. and Webb, J. () Moessbauer spectroscopic studies of hemerythrin from Phascolosoma lurco (syn.

Phascolosoma Arcuatum). Biochemistry, 20 (16). Webb, J. and Chrystal, P. () Protein binding of iron in blood plasma of the ascidian. Mossbauer spectroscopic and magnetic measurements have been made on a novel magnetic protein produced by the controlled reconstitution of ferritin.

The data indicate that the predominant mineral form in the iron-containing cores is maghemite (y-Fe) rather than magnetite (Fe)' 1. Introduction. For example, previous studies using anionic nanoparticles report iron levels of 10 pg per cell after a minute incubation period with 5 mM iron.

38 In comparison, incubation with a cationized magnetoferritin solution containing μM protein corresponds to incubation with approximately mM iron and also yields approximately 10 pg of iron Cited by: 1. Kinetic and CD/MCD Spectroscopic Studies of the Atypical, Three-His-Ligated, Non-Heme Fe 2+ Center in Diketone Dioxygenase: The Role of Hydrophilic Outer Shell Residues in Catalysis Grit D.

Straganz, Adrienne R. Diebold, Sigrid Egger, Bernd Nidetzky and Edward I. Solomon. Medical definition of apoferritin: a colorless crystalline protein capable of storing iron in bodily cells especially of the liver by combining with iron to form ferritin.

PbS nanocrystals entrapped in the hollow core of apoferritin protein cages are synthesized in aqueous solution by both reassembly and nanoreactor routes. In both cases, apoferritin limits the size of the PbS quantum dot it can encapsulate to 8 nm and provides a route to the creation of a stable near‐infrared fluorescent composite.

hand, apoferritin molecules are all identical and have a roughly spherically symmetric structure giving rise to Bessel-like function oscillations in the SAXS data The difference between holoferritin and apoferritin can be seen in Figs. 1 a and 1 b. Also shown in Fig. 1 c is the SAXS data from ferritin to which was added 90 mM CdCl 2 salt.

The proceedings of the 11th Zeolite Conference has been published in three volumes, containing 5 plenary lectures and full papers. Part A comprises Synthesis and Characterization (99 papers), Part B Catalysis and Environment ( papers) and Part C Adsorption and Diffusion, Modifications, Novel Materials and Theory (78 papers).

Special Issue "Magnetic Nanoparticles " Special Issue Editors magnetic measurements, thermal analysis and infrared spectroscopic studies. X-ray diffraction and TEM results demonstrated that the magnetic doxorubicin encapsulation into the apoferritin and its conjugation with magnetic particles was investigated by capillary.

Studies are also being conducted to better understand its utility in chemo-enzymatic syntheses (Bolt et al.and Calveras et al. ), its interactions with other cellular proteins (Forlemu et al. ), and its reaction intermediates (St.-Jean et al. The iron storage protein ferritin consists of a spherical polypeptide shell (apoferritin) surrounding a 6-nanometer inorganic core of the hydrated iron oxide ferrihydrite (5Fe 2 O 3 9H 2 O).

Previous studies have shown that the in vitro reconstitution of apoferritin yields mineral cores essentially identical to those of the native proteins.

Apoferritin structure • Ferritin was first discovered in by Laufberger • in most living organisms, used to store iron ions ( iron atoms) • Apoferritin – removal of iron by dithionite or thioglycolate (reducing agent) • Apoferritin - protein with cage like structure • 24 polypeptide subunits • cavity about 8.

apoferritin and on the production of ferritin and apoferritin by two cell lines derived from human cancers and grow-ing in vitro in defined media.

Using modifications of the staining procedure with uranyl nitrate, he has found that the apoferritin shell of the ferritin molecule is composed of 20 equal subunits with diameters in the neigh-Cited by: 4. (biochemistry) Ferritin that is not combined with iron Definition from Wiktionary, the free dictionary.

VOL NUMBER 6 PHYSICAL REVIEW LETTERS 7FEBRUARY Evidence for Non-DLVO Hydration Interactions in Solutions of the Protein Apoferritin Dimiter N. Petsev1 and Peter G. Vekilov1,2 1Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 2Department of Chemistry, University of Alabama in Huntsville, Huntsville, Alabama.

Serge Lefrant, Mihaela Baibarac and Ioan Baltog, Spectroscopic Studies on Nanocomposites Obtained by Functionalization of Carbon Nanotubes with Conducting Polymers, Molecular Crystals and Liquid Crystals,1, (75/[]), ().Cited by: L-Leucine, also known as 2-Aminomethylpentanoic acid, is a component of the subunits in astacin, ferritin, and other buffer proteins.

Ungraded products supplied by Spectrum are indicative of a grade suitable for general industrial use. Table 2D-crystallization screen. A, Conditions: 1 mg/mL apoferritin, 50 mM Na-acetate, pHmM NaCl, 10 mM NaN3.

B, Conditions: 8 mg/mL apoferritin, 50 mM Tris-HCl, pHmM NaCl, 10 mM NaN3. The temperature increments are equal in size: the unequal representation is due to by: 1. Spectroscopic Determination of Iron in Vitamin Tablets (1) Transfer mL of standard iron solution to a mL volumetric flask.

Add mL of hydroxylamine, mL of sodium acetate, and mL of 1,phenanthroline to the flask. Allow the mixture to stand for 5 min; dilute to the mark and mix well. Calculate the concentrationFile Size: 34KB. Posts about Apoferritin written by Avinash Deo. Ferritin Ferritin is made of apoferritin and iron.

Apoferritin is a protein shell made of 24 subunits that is 13nm in diameter. in the liver as ferritin (iron w/ apoferritin coating) can also be found in blood. what is a good indicator of iron stores in "healthy people" serum ferritin measurement can increase in liver disease, infection, inflammation, or iron excess.

UIBC. the amount of iron that could bind to transferrin (about ug/dl). @article{osti_, title = {Kinetics of α-MnOOH Nanoparticle Formation through Enzymatically Catalyzed Biomineralization inside Apoferritin}, author = {Hui, Yue and Jung, Haesung and Kim, Doyoon and Jun, Young-Shin}, abstractNote = {While biomineralization in apoferritin has effectively synthesized highly monodispersed nanoparticles of various metal oxides and hydroxides, the detailed.Publications: St Pierre, Timothy Stats for St Pierre, Timothy Export as ASCII Citation BibTeX Dublin Core EP3 XML EndNote HTML Citation JSON METS Multiline CSV Object IDs OpenURL ContextObject RDF+N-Triples RDF+N3 RDF+XML RefWorks Refer Reference Manager.Micelle-mediated transport-the correct answer is c.

this patient has vitamin a deficiency, which is characterized by early symptoms of night blindness, dry conjunctivae, and gray plaques, or late symptoms of corneal ulceration and necrosis leading to perforation and blindness.

this deficiency is typically seen in children and pregnant women whose diets are deficient in vitamin a, especially.