Structural organization of C-terminal parts of fibrinogen Aα-chains

Structural organization of C-terminal parts of fibrinogen Aα-chains

Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.

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Bibliographische Detailangaben
Veröffentlicht in:FEBS letters 1983-08, Vol.160 (1), p.291-295
Hauptverfasser: Medved', L.V., Gorkun, O.V., Privalov, P.L.
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Aα-chain
Biological and medical sciences
Blood coagulation. Blood cells
Calorimetry
Cattle
Coagulation factors
Domain
Fibrinogen
Fibrinolysin
Fibrinopeptide A
Fundamental and applied biological sciences. Psychology
Macromolecular Substances
Molecular and cellular biology
Peptide Fragments - analysis
Protein Conformation
Thermodynamics
Unfolding
X-fragment
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Beschreibung
Zusammenfassung:Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80985-5