Domain organization of the terminal parts in the fibrinogen molecule.
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.
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
D046911:Macromolecular Substances; D010446:Peptide Fragments; D005340:Fibrinogen; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin; D010434:Pepsin A