Longitudinal orientation of cross-linked polypeptide γ chains in fibrin fibrils.
Dokl Biochem Biophys
; 464: 286-9, 2015.
Article
em En
| MEDLINE
| ID: mdl-26518549
ABSTRACT
The crosslinking of fibrin γ-polypeptide chains under the influence of the plasma fibrin-stabilizing factor (FXIIIa), which causes their conversion to γ-γ dimers, is the major enzyme reaction of covalent fibrin stabilization. We studied the self-assembly of soluble cross-linked fibrin oligomers. The results of analytical ultracentrifugation as well as elastic and dynamic light scattering showed that the double-stranded fibrin oligomers formed under the influence of moderate concentrations of urea are cross-linked only due to formation of γ-γ dimers, which can dissociate into single-stranded structure when the concentration of urea increases. This fact proves that γ-γ dimers are formed in the end-to-end manner.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fibrina
Limite:
Humans
Idioma:
En
Revista:
Dokl Biochem Biophys
Assunto da revista:
BIOFISICA
/
BIOQUIMICA
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Federação Russa