Characterisation of iron binding ligands in seawater by reverse titration

Analytica Chimica Acta ◽

10.1016/j.aca.2012.12.048 ◽

2013 ◽

Vol 766 ◽

pp. 53-60 ◽

Author(s):

Jeffrey A. Hawkes ◽

Martha Gledhill ◽

Douglas P. Connelly ◽

Eric P. Achterberg

Keyword(s):

Iron Binding ◽

Reverse Titration

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An iron-binding component in human blood plasma

The Journal of Trace Elements in Experimental Medicine ◽

10.1002/jtra.1017 ◽

2001 ◽

Vol 14 (2) ◽

pp. 111-113

Author(s):

Arthur L. Schade ◽

Liona Caroline

Keyword(s):

Blood Plasma ◽

Human Blood ◽

Human Blood Plasma ◽

Iron Binding ◽

Binding Component

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The Role of the Interaction between Fe(III) and Cell Surface in the Accumulation of 67Ga by Tumor Cells

Nuklearmedizin ◽

10.1055/s-0038-1629590 ◽

1991 ◽

Vol 30 (06) ◽

pp. 290-293 ◽

Author(s):

P. Maleki ◽

A. Martinezi ◽

M. C. Crone-Escanye ◽

J. Robert ◽

L. J. Anghileri

Keyword(s):

Cell Surface ◽

Tumor Cells ◽

Ionic Composition ◽

Iron Complex ◽

Iron Binding ◽

Complex Time ◽

Interaction Product ◽

Thermodynamic Constant ◽

Number Of Cells

The study of the interaction between complexed iron and tumor cells in the presence of 67Ga-citrate indicates that a phenomenon of iron-binding related to the thermodynamic constant of stability of the iron complex, and a hydrolysis (or anion penetration) of the interaction product determine the uptake of 67Ga. The effects of various parameters such as ionic composition of the medium, nature of the iron complex, time of incubation and number of cells are discussed.

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Faculty Opinions recommendation of The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1004064.191655 ◽

2003 ◽

Author(s):

Elizabeth Theil

Keyword(s):

Crystal Structure ◽

Agrobacterium Tumefaciens ◽

Hydroxyl Radical ◽

Radical Scavenging ◽

Oxidative Cleavage ◽

Iron Binding ◽

X Ray ◽

Radical Scavenging Properties ◽

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Faculty Opinions recommendation of The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1033739.387940 ◽

2006 ◽

Author(s):

James Penner-Hahn

Keyword(s):

Binding Motif ◽

Iron Binding ◽

Iron Sulfur Cluster ◽

Sulfur Cluster ◽

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Faculty Opinions recommendation of Analysis of RNA Methylation by Phylogenetically Diverse Cfr Radical S-Adenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.736065311.793573054 ◽

2020 ◽

Author(s):

Sheila David

Keyword(s):

Iron Binding ◽

Rna Methylation ◽

Accessory Domain

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Manufacturing of Iron Binding Peptide Using Sericin Hydrolysate and Its Bioavailability in Iron Deficient Rat

Journal of the Korean Society of Food Science and Nutrition ◽

10.3746/jkfn.2010.39.10.1446 ◽

2010 ◽

Vol 39 (10) ◽

pp. 1446-1451 ◽

Author(s):

Hye-Jin Cho ◽

Hyun-Sun Lee ◽

Eun-Young Jung ◽

So-Yeon Park ◽

Woo-Taek Lim ◽

...

Keyword(s):

Iron Binding ◽

Binding Peptide ◽

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A study on the iron binding protein of plasma

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19490287 ◽

1949 ◽

Vol 14 ◽

pp. 287-303 ◽

Author(s):

S. Fiala

Keyword(s):

Binding Protein ◽

Iron Binding ◽

Iron Binding Protein

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Self-Assembly and Biphasic Iron-Binding Characteristics of Mms6, A Bacterial Protein That Promotes the Formation of Superparamagnetic Magnetite Nanoparticles of Uniform Size and Shape

Biomacromolecules ◽

10.1021/bm201278u ◽

2011 ◽

Vol 13 (1) ◽

pp. 98-105 ◽

Author(s):

Lijun Wang ◽

Tanya Prozorov ◽

Pierre E. Palo ◽

Xunpei Liu ◽

David Vaknin ◽

...

Keyword(s):

Magnetite Nanoparticles ◽

Self Assembly ◽

Iron Binding ◽

Bacterial Protein ◽

Uniform Size ◽

Binding Characteristics ◽

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A newly identified iron binding protein in duodenal mucosa of rats. Purification and characterization of mobilferrin.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)34117-1 ◽

1990 ◽

Vol 265 (9) ◽

pp. 5273-5279

Author(s):

M E Conrad ◽

J N Umbreit ◽

E G Moore ◽

R D Peterson ◽

M B Jones

Keyword(s):

Binding Protein ◽

Duodenal Mucosa ◽

Iron Binding ◽

Purification And Characterization ◽

Iron Binding Protein

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Structure and function of ovotransferrin. II. Iron-transferring activity of iron-binding fragments of ovotransferrin with chicken embryo red cells.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)68172-x ◽

1982 ◽

Vol 257 (3) ◽

pp. 1184-1188 ◽

Author(s):

W.M. Keung ◽

P. Azari

Keyword(s):

Chicken Embryo ◽

Structure And Function ◽

Red Cells ◽

Iron Binding ◽

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