title: Domain organization of the terminal parts in the fibrinogen molecule.
abstract: Using limited proteolysis and scanning microcalorimetry it was shown that each terminal part of the fibrinogen molecule is constituted by four co-operative domains. Among these domains two strongly interacting domains are formed by the C-terminal part of the beta-chain, while the two other domains are formed by the C-terminal part of the gamma-chain.
mesh_terms: D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000032:analysis*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D013816:Thermodynamics; D014357:Trypsin / Q000378:metabolism
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D005340:Fibrinogen; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin; D010434:Pepsin A