Selective reduction of a disulphide bridge in hen ovotransferrin.
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.
D000478:Alkylation; D000818:Animals; D002645:Chickens; D003207:Conalbumin / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004527:Egg Proteins / Q000378:metabolism*; D005260:Female; D007501:Iron / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D014508:Urea / Q000378:metabolism
D004220:Disulfides; D004527:Egg Proteins; D010446:Peptide Fragments; D003207:Conalbumin; D014508:Urea; D007501:Iron; D003545:Cysteine; D004229:Dithiothreitol