Mutations at the Histidine 249 Ligand Profoundly Alter the Spectral and Iron-Binding Properties of Human Serum Transferrin N-Lobe†

Biochemistry ◽  
2000 ◽  
Vol 39 (6) ◽  
pp. 1205-1210 ◽  
Author(s):  
Qing-Yu He ◽  
Anne B. Mason ◽  
Rowchanak Pakdaman ◽  
N. Dennis Chasteen ◽  
Bonnie K. Dixon ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Binding Properties ◽  
Human Serum Transferrin

scholarly journals The C2 variant of human serum transferrin retains the iron binding properties of the native protein

2005 ◽  
Vol 1741 (3) ◽  
pp. 264-270 ◽  
Author(s):  
Paolo Zatta ◽  
Luigi Messori ◽  
Pierluigi Mauri ◽  
Susan J. van Rensburg ◽  
Johann van Zyl ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Native Protein ◽  
Binding Properties ◽  
Human Serum Transferrin

The glycation site specificity of human serum transferrin is a determinant for transferrin's functional impairment under elevated glycaemic conditions

2014 ◽  
Vol 461 (1) ◽  
pp. 33-42 ◽  
Author(s):  
André M. N. Silva ◽  
Paulo R. H. Sousa ◽  
João T. S. Coimbra ◽  
Natércia F. Brás ◽  
Rui Vitorino ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Amino Acid ◽  
Human Serum ◽  
Serum Transferrin ◽  
Site Specificity ◽  
Iron Binding ◽  
Amino Acid Residues ◽  
Human Serum Transferrin ◽  
Structural Alterations ◽  
Iron Binding Protein

Human serum transferrin is susceptible to modification under elevated glycaemic conditions, such as those encountered in diabetes mellitus. The study of transferrin glycation shows that key amino acid residues undergo glycation, inducing structural alterations that compromise its function as an iron-binding protein.

Effects of Mutations of Aspartic Acid 63 on the Metal-Binding Properties of the Recombinant N-Lobe of Human Serum Transferrin†

Biochemistry ◽  
1997 ◽  
Vol 36 (18) ◽  
pp. 5522-5528 ◽  
Author(s):  
Qing-Yu He ◽  
Anne B. Mason ◽  
Robert C. Woodworth ◽  
Beatrice M. Tam ◽  
Toby Wadsworth ◽  
...  
Keyword(s):  
Human Serum ◽  
Aspartic Acid ◽  
Metal Binding ◽  
Serum Transferrin ◽  
Binding Properties ◽  
Human Serum Transferrin

scholarly journals Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein

1978 ◽  
Vol 173 (2) ◽  
pp. 543-552 ◽  
Author(s):  
R W Evans ◽  
J Williams
Keyword(s):  
Amino Acid ◽  
Human Serum ◽  
Terminal Region ◽  
The Other ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Proteolytic Digestion ◽  
Human Serum Transferrin ◽  
Partially Saturated ◽  
Peptide Maps

1. Trypsin digestion of human serum transferrin partially saturated with iron(III)-nitrilotriacetate at pH 5.5 or pH 8.5 produces a carbohydrate-containing iron-binding fragment of mol.wt. 43000. 2. When iron(III) citrate, FeCl3, iron (III) ascorabate and (NH4)2SO4,FeSO4 are used as iron donors to saturate the protein partially, at pH8.5, proteolytic digestion yields a fragment of mol.wt. 36000 that lacks carbohydrate. 3. The two fragments differ in their antigenic structures, amino acid compositions and peptide ‘maps’. 4. The fragment with mol.wt. 36000 was assigned to the N-terminal region of the protein and the other to the C-terminal region. 5. The distribution of iron in human serum transferrin partially saturated with various iron donors was examined by electrophoresis in urea/polyacrylamide gels and the two possible monoferric forms were unequivocally identified. 6. The site designated A on human serum transferrin [Harris (1977) Biochemistry 16, 560–564] was assigned to the C-terminal region of the protein and the B site to the N-terminal region. 7. The distribution of iron on transferrin in human plasma was determined.

A Density Functional Theory Study of the Iron-Binding Site of Human Serum Transferrin

2004 ◽  
Vol 57 (12) ◽  
pp. 1219 ◽  
Author(s):  
David Rinaldo ◽  
Martin J. Field
Keyword(s):  
Human Serum ◽  
Binding Site ◽  
Conformational Changes ◽  
Metal Binding ◽  
Density Functional ◽  
Release Mechanism ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Iron Release ◽  
Human Serum Transferrin

Human serum transferrin binds ferric ions with high affinity in the blood stream and releases them into cells by a process involving receptor-mediated endocytosis and a decrease in pH. The iron-release mechanism is unclear but protonation events and conformational changes are known to be important. In this study, we investigate properties of the iron-binding site theoretically. Our results suggest that an equatorial histidine could be in its histidinate form when bound to iron at neutral and high pH and that protonation of an axial tyrosine is a key event in iron release. Support for this mechanism from other metal-binding enzymes is also presented.

scholarly journals The binding properties of some novel ruthenium (III) complexes with human serum transferrin

2011 ◽  
Vol 27 (2) ◽  
pp. 141-146 ◽  
Author(s):  
A. L. Arsene ◽  
V. Uivarosi ◽  
N. Mitrea ◽  
C. M. Dragoi ◽  
A. Nicolae
Keyword(s):  
Human Serum ◽  
Serum Transferrin ◽  
Binding Properties ◽  
Human Serum Transferrin

scholarly journals The electrophoresis of transferrins in urea/polyacrylamide gels

1980 ◽  
Vol 189 (3) ◽  
pp. 541-546 ◽  
Author(s):  
R W Evans ◽  
J Williams
Keyword(s):  
Human Serum ◽  
Binding Capacity ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Polyacrylamide Gels ◽  
Human Serum Transferrin ◽  
Free Protein ◽  
Iron Binding Capacity ◽  
Terminal Domains

The denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss of iron-binding capacity and (c) u.v. difference spectrometry. In human serum transferrin and hen ovotransferrin the N-terminal and C-terminal domains of the iron-free protein were found to denature at different urea concentrations.

scholarly journals A first-principles study on potential chelation agents and indicators of Alzheimer's disease

RSC Advances ◽  
2020 ◽  
Vol 10 (58) ◽  
pp. 35574-35581
Author(s):  
Bryan Wang ◽  
Xuan Luo
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Human Serum ◽  
Blood Brain Barrier ◽  
First Principles ◽  
Brain Barrier ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
First Principles Study ◽  
Blood Brain

Human-serum transferrin is involved in the transportation of aluminum across the blood–brain barrier.

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