Paper Information

Title: 

BACTERIAL EXPRESSION OF A SUBFRAGMENT OF HUMAN FACTOR VIII HEAVY-CHAIN IN ESCHERICHIA COLI

Type: PAPER
Author(s): AMIRZADEH N.,ZOMORODIPOUR A.R.*,POURFATH ELAH A.A.,ATAEI FARIBA
 
 *DEPARTEMNT OF MOLECULAR GENETICS, NATIONAL INSTITUTE FOR GENETIC ENGINEERING & BIOTECHNOLOGY, IRAN, TEHRAN
 
Name of Seminar: NATIONAL CONGRESS OF BIOTECHNOLOGY OF IRAN
Type of Seminar:  CONGRESS
Sponsor:  IRANIAN BIOTECHNOLOGY ASSOCIATION
Date:  2005Volume 4
 
 
Abstract: 

Human factor VIII (hFVIII) plays a major role in the intrinsic pathway of blood coagulation. The absence or malfunction of FVIII is associated with the X-linked recessive bleeding disorder; known as haemophilia A. A number of these patients, who are routinely treated with the hFVIII infusion therapy, develop antibodies that inhibit hFVIII activity. Bacterially produced FVIII-epitopes are capable to neutralize the alloantibodies. The purpose of present study was to express a subfragmment of FVIII heavy chain in E.coli. with this goal, A 1640 bp DNA fragment from heavy-chain of hFVIII was inserted in a T7-based expression vector followed by the transformation of BL21 (DE3) strain of E. coli. The use of His6-tagged tail was also considered for purification purpose. Among the total proteins of the isolated clones, a protein was expressed that was detectable with anti-hFVIII-heavy chain monoclonal antibody. Due to low expression level of the A1A2-related protein, its efficient purification was not possible. Further attempts are required for optimization of the expression of sub fragments from hFVIII-heavy chain.

 
Keyword(s): HFVIII, HEAVY CHAIN, A1A2 DOMAIN, E.COLI
 
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