Human coagulation factor VIII domain-specific recombinant polypeptide expression
Blood Research
;
: 103-108, 2015.
Article
in English
| WPRIM
| ID: wpr-184126
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Peptides
/
Bacteria
/
Blood Coagulation
/
Factor IX
/
Factor VIII
/
Chromatography, Affinity
/
Clone Cells
/
Hepatocytes
/
Glutathione Transferase
/
Hemophilia A
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
Blood Research
Year:
2015
Type:
Article
Similar
MEDLINE
...
LILACS
LIS