Fibrinogen Detroit - an abnormal fibrinogen with non-functional NH2-terminal polymerization domain
| Autor: | Margareta Blombäck, Birger BIombäck, Bohdan Kudryk |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Immunodiffusion
Non functional Abnormal fibrinogen medicine.disease_cause Fibrinogen Chromatography Affinity Structure-Activity Relationship Dogs Thrombin medicine Animals Humans Disulfides Blood Coagulation Immunoelectrophoresis Mutation Binding Sites Fibrinogen Detroit Chemistry Hematology Blood Coagulation Disorders Peptide Fragments Polymerization Biochemistry medicine.drug Conjugate |
| Zdroj: | Thrombosis Research. 9:25-36 |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/0049-3848(76)90146-8 |
| Popis: | Fibrinogen Detroit was found to have affinity for thrombin activated fibrinogen-Sepharose conjugates prepared from normal fibrinogen. On the other hand, thrombin activated fibrinogen-Sepharose conjugates prepared from fibrinogen Detroit did not, to any appreciable extent, bind normal fibrinogen nor the plasmic degradation product, Fragment D. It is concluded that the N-DSK domain in fibrinogen Detroit, containing the mutation (Aα 19 Arg → Ser), is abnormal with regard to binding whereas the Fragment D domain has normal binding properties. |
| Databáze: | OpenAIRE |
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