Selective reduction of a disulphide bridge in hen ovotransferrin. 1985

J Williams, and K Moreton, and A D Goodearl

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.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011489 Protein Denaturation Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D003207 Conalbumin A glycoprotein albumin from hen's egg white with strong iron-binding affinity. Ovotransferrin
D003545 Cysteine A thiol-containing non-essential amino acid that is oxidized to form CYSTINE. Cysteine Hydrochloride,Half-Cystine,L-Cysteine,Zinc Cysteinate,Half Cystine,L Cysteine
D004220 Disulfides Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties. Disulfide
D004229 Dithiothreitol A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols. Cleland Reagent,Cleland's Reagent,Sputolysin,Clelands Reagent,Reagent, Cleland,Reagent, Cleland's

Related Publications

J Williams, and K Moreton, and A D Goodearl
June 1992, Journal of molecular biology,
J Williams, and K Moreton, and A D Goodearl
February 1982, European journal of biochemistry,
J Williams, and K Moreton, and A D Goodearl
November 1995, Journal of molecular biology,
J Williams, and K Moreton, and A D Goodearl
June 1975, The Biochemical journal,
J Williams, and K Moreton, and A D Goodearl
May 2001, Journal of computer-aided molecular design,
J Williams, and K Moreton, and A D Goodearl
December 2011, Cell biochemistry and biophysics,
J Williams, and K Moreton, and A D Goodearl
June 1968, The Biochemical journal,
J Williams, and K Moreton, and A D Goodearl
June 1975, The Biochemical journal,
J Williams, and K Moreton, and A D Goodearl
July 1975, The Biochemical journal,
J Williams, and K Moreton, and A D Goodearl
December 1998, Journal of molecular biology,
Copied contents to your clipboard!