Conformational identity of human fibrinogen and monomeric fibrin
| Autor: | Pierre Wiltzius, Victor Hofmann |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Light
Protein Conformation Fibrinopeptide B Fibrinogen Fibrin chemistry.chemical_compound Thrombin Protein structure Dynamic light scattering medicine Humans Scattering Radiation Fibrinopeptide A biology Batroxobin Rotational diffusion Hematology Monomer chemistry Biochemistry biology.protein Biophysics medicine.drug |
| Zdroj: | Thrombosis Research. 19:793-798 |
| ISSN: | 0049-3848 |
| Popis: | Human monomeric fibrin kept in solution in acidic buffer after thrombin or Reptilase proteolysis was compared to fibrinogen in physiological and acidic buffer by means of dynamic light scattering. The translational and rotational diffusion coefficients of the two monomeric solutions did not significantly deviate from those of fibrinogen in physiological or acidic buffer. It is therefore concluded that no major conformational modification occurs upon release of the fibrinopeptides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|