scholarly journals Iron-binding fragments from the N-terminal and C-terminal regions of human lactoferrin

1978 ◽  
Vol 171 (2) ◽  
pp. 321-327 ◽  
Author(s):  
J M Bluard-Deconinck ◽  
J Williams ◽  
R W Evans ◽  
J van Snick ◽  
P A Osinski ◽  
...  
Keyword(s):  
Cross Reaction ◽  
Human Lactoferrin ◽  
Iron Binding ◽  
Native Protein ◽  
Terminal Part ◽  
Immunological Cross Reaction

Digestion of lactoferrin with pepsin at pH3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%-iron-saturated lactoferrin yielded the N- and C-terminal half molecules, which could be separated by DEAE-Sephadex chromatography. The N- and C-terminal fragments did not show any immunological cross-reaction. The carbohydrate of lactoferrin was distributed equally between the two fragments.

scholarly journals Selective reduction of a disulphide bridge in hen ovotransferrin

1985 ◽  
Vol 228 (3) ◽  
pp. 661-665 ◽  
Author(s):  
J Williams ◽  
K Moreton ◽  
A D Goodearl
Keyword(s):  
Selective Reduction ◽  
Iron Binding ◽  
Thiol Groups ◽  
Native Protein ◽  
Brief Treatment ◽  
Disulphide Bridge ◽  
Binding Properties ◽  
Terminal Domain ◽  
Fluorescent Derivative

Brief treatment of iron-saturated hen ovotransferrin with dithiothreitol selectively cleaves the disulphide bridge between residues 478 and 671, which is in the C-terminal domain of the protein. The reduced alkylated protein is less stable than the native protein, and its iron-binding properties are different. A fluorescent derivative was prepared by coupling N-iodoacetyl-N'-(5-sulpho-1-naphthyl)ethylenediamine to the thiol groups.

scholarly journals Structural aspects of human lactoferrin in the iron-binding process studied by molecular dynamics and small-angle neutron scattering

2018 ◽  
Vol 41 (9) ◽  
Author(s):  
Lilia Anghel ◽  
Aurel Radulescu ◽  
Raul Victor Erhan
Keyword(s):  
Molecular Dynamics ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
The Body ◽  
Human Lactoferrin ◽  
Radius Of Gyration ◽  
Scattering Method ◽  
Iron Binding ◽  
Binding Process

Abstract. Lactoferrin is a non-heme protein known for its ability to bind tightly Fe(III) ions in various physiological environments. Due to this feature lactoferrin plays an important role in the processes of iron regulation at the cellular level preventing the body from damages produced by high levels of free iron ions. The X-ray crystal structure of human lactoferrin shows that the iron-binding process leads to conformational changes within the protein structure. The present study was addressed to conformation stability of human lactoferrin in solution. Using molecular dynamics simulations, it was shown that Arg121 is the key amino acid in the stabilization of the Fe(III) ion in the N-lobe of human lactoferrin. The small-angle neutron scattering method allowed us to detect the structural differences between the open and closed conformation of human lactoferrin in solution. Our results indicate that the radius of gyration of apolactoferrin appears to be smaller than that of the hololactoferrin, $R_{g}=24.16(\pm 0.707)$ R g = 24 . 16 ( ± 0 . 707 ) Å and $R_{g}= 26.20(\pm 1.191)$ R g = 26 . 20 ( ± 1 . 191 ) Å, respectively. The low-resolution three-dimensional models computed for both forms of human lactoferrin in solution also show visible differences, both having a more compact conformation compared to the high-resolution structure. Graphical abstract

Altered Domain Closure and Iron Binding in Transferrins: The Crystal Structure of the Asp60Ser Mutant of the Amino-terminal Half-molecule of Human Lactoferrin

1996 ◽  
Vol 256 (2) ◽  
pp. 352-363 ◽  
Author(s):  
Rick H. Faber ◽  
Tony Bland ◽  
Catherine L. Day ◽  
Gillian E. Norris ◽  
John W. Tweedie ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Human Lactoferrin ◽  
Iron Binding ◽  
Amino Terminal
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