title: Disulphide bridges of bovine factor X.
abstract: Evidence is presented for the disulphide bridges in bovine Factor X. The protein was degraded by chemical and enzymic means, and all 12 disulphide bridges were isolated in separate peptides except for bridges nos. 6/7 in the light chain. All the disulphide bridges were found to be in positions corresponding to those found in other homologous domains. This report is the first verification of an epidermal-growth-factor-homologous domain having the same disulphide-bonding pattern as that found in mouse epidermal growth factor.
authors: Department of Molecular Biology and Plant Physiology, University of Aarhus, Denmark.
authors: P
authors: P
authors: Højrup
authors: S
authors: S
authors: Magnusson
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D004220:Disulfides / Q000032:analysis*; D005170:Factor X; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D000596:Amino Acids; D004220:Disulfides; D010446:Peptide Fragments; D005170:Factor X