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 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

scholarly journals Expression, Purification, and Metal Binding Properties of the N-terminal Domain from the Wilson Disease Putative Copper-transporting ATPase (ATP7B)

1997 ◽  
Vol 272 (52) ◽  
pp. 33279-33282 ◽  
Author(s):  
Michael DiDonato ◽  
Suree Narindrasorasak ◽  
John R. Forbes ◽  
Diane W. Cox ◽  
Bibudhendra Sarkar
Keyword(s):  
Metal Binding ◽  
Wilson Disease ◽  
Binding Properties ◽  
Terminal Domain

The iron-binding properties of gastric juice

1969 ◽  
Vol 24 (1) ◽  
pp. 87-92 ◽  
Author(s):  
A. Jacobs ◽  
P.M. Miles
Keyword(s):  
Gastric Juice ◽  
Iron Binding ◽  
Binding Properties

scholarly journals Impact of copper and iron binding properties on the anticancer activity of 8-hydroxyquinoline derived Mannich bases

2018 ◽  
Vol 47 (47) ◽  
pp. 17032-17045 ◽  
Author(s):  
Veronika F. S. Pape ◽  
Nóra V. May ◽  
G. Tamás Gál ◽  
István Szatmári ◽  
Flóra Szeri ◽  
...  
Keyword(s):  
Anticancer Activity ◽  
Mannich Bases ◽  
Iron Binding ◽  
Binding Properties

A relationship between pKa values, binding abilities to copper(ii) and iron(iii) and anticancer activity of 8-hydroxyquinoline derived Mannich bases.

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 The covalent nature of the human antithrombin III–thrombin bond

1980 ◽  
Vol 189 (3) ◽  
pp. 481-489 ◽  
Author(s):  
M O Longas ◽  
T H Finlay
Keyword(s):  
Gel Electrophoresis ◽  
Antithrombin Iii ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Native Protein ◽  
Disulphide Bridge ◽  
Terminal Amino Acid ◽  
Carboxypeptidase B ◽  
Terminal Amino ◽  
Covalent Nature

1. Cleavage of the human antithrombin III–thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. 2. Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction. The heavy band has the electrophoretic mobility of the native protein. The light band has an apparent mol.wt. that is approx. 4000 less than the molecular weight of native antithrombin III. 3. Treatment of the cleavage products of the complex with carboxypeptidase B yields 1 mumol of arginine, a new C-terminal amino acid, per mumol of thrombin dissociated. The results indicate that during formation of the antithrombin III–thrombin complex, the inhibitor is cleaved at an arginine–X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s).

Iron‐Binding Properties of TTf, a Salt‐Induced Transferrin from the Alga Dunaliella salina

2003 ◽  
Vol 26 (10-11) ◽  
pp. 2081-2091 ◽  
Author(s):  
Michal Schwarz ◽  
Ada Zamir ◽  
Uri Pick
Keyword(s):  
Dunaliella Salina ◽  
Iron Binding ◽  
Binding Properties

scholarly journals The effect of salt concentration on the iron-binding properties of human transferrin

1982 ◽  
Vol 201 (3) ◽  
pp. 527-532 ◽  
Author(s):  
J Williams ◽  
N D Chasteen ◽  
K Moreton
Keyword(s):  
Salt Concentration ◽  
Binding Sites ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Iron Binding ◽  
Iron Release ◽  
Equilibrium Conditions ◽  
Binding Properties ◽  
Kinetics Of ◽  
Terminal Site

The salt dependence of the iron-binding properties of transferrin was studied by urea/polyacrylamide-gel electrophoresis. The distribution of iron between the N-terminal and C-terminal binding sites under equilibrium conditions and the rates of release of iron from the two sites were studied. It was found that salt increases the thermodynamic stability of iron binding in the N-terminal site relative to the C-terminal site. Similar behaviour is observed for the kinetics of iron release, where salt retards the rate of removal of iron from the N-terminal site but facilitates removal from the C-terminal site.

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