[Domainal organization of the molecules of Lys-plasminogen].
The intramolecular melting of the human Lys-plasminogen and its different fragments were studied by the differential scanning microcalorimetry method. Thermodynamical analysis of melting curves showed that the Lys-plasminogen molecule consists of 7 domains. Five of them are formed by five homologeus regions of the polypeptide chain (kringle), while two domains are formed by the part of the polypeptide chain corresponding to the plasmin light chain. The domains included in the fragments seem to be rather independent, since fragmentation does not lead to noticeable changes of their stability in comparison to that of the intact molecule. It has been shown also that plasminogen-plasmin conversion is accompanied by structural transformation of the molecule which results in the destabilization of one of the light chain domains.
D002152:Calorimetry, Differential Scanning; D005341:Fibrinolysin / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D010196:Pancreatic Elastase; D010446:Peptide Fragments / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation
D046911:Macromolecular Substances; D010446:Peptide Fragments; C018998:lysyl-plasminogen; D010958:Plasminogen; D010196:Pancreatic Elastase; D005341:Fibrinolysin
Domennaia organizatsiia molekuly Lys-plazminogena.