Human coagulation factor VIII domain-specific recombinant polypeptide expression
Blood Research
; : 103-108, 2015.
Artigo
em Inglês
| WPRIM (Pacífico Ocidental)
| ID: wpr-184126
Biblioteca responsável:
WPRO
ABSTRACT
BACKGROUND:
Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners.METHODS:
To determine F8 domain-specific functions during blood coagulation, the FVIII domains A1, A2, A3, and C were cloned from Hep3B hepatocytes. Domain-specific recombinant polypeptides were glutathione S-transferase (GST)- or polyhistidine (His)-tagged, over-expressed in bacteria, and purified by specific affinity chromatography.RESULTS:
Recombinant polypeptides of predicted sizes were obtained. The GST-tagged A2 polypeptide interacted with coagulation factor IX, which is known to bind the A2 domain of activated FVIII.CONCLUSION:
Recombinant, domain-specific polypeptides are useful tools to study the domain-specific functions of FVIII during the coagulation process, and they may be used for production of domain-specific antibodies.
Texto completo:
Disponível
Base de dados:
WPRIM (Pacífico Ocidental)
Assunto principal:
Peptídeos
/
Bactérias
/
Coagulação Sanguínea
/
Fator IX
/
Fator VIII
/
Cromatografia de Afinidade
/
Células Clonais
/
Hepatócitos
/
Glutationa Transferase
/
Hemofilia A
Tipo de estudo:
Estudo prognóstico
Limite:
Humanos
Idioma:
Inglês
Revista:
Blood Research
Ano de publicação:
2015
Tipo de documento:
Artigo