Mass Production and Characterization of Anti-HBsAg Human Antibody B7 Fd.
- Author:
In Hak CHOI
;
Ik Jung KIM
;
Jun Ho CHUNG
;
Suk Jin CHOI
;
Jong Bum IM
;
Kye Sook YI
;
Pann Ghill SUH
;
Sung Ho RYU
- Publication Type:Original Article
- MeSH:
Antigens, Surface;
Enzyme-Linked Immunosorbent Assay;
Guanidine;
Hepatitis B virus;
Humans*;
Immunoglobulin G;
Inclusion Bodies
- From:Journal of the Korean Society for Microbiology
1999;34(3):265-275
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
We expressed anti-HBsAg human antibody fragment (B7 Fd) using pRSET-A vector and BL21(DE3)pLysS strain of E. coli. B7 Fd is composed only of variable domain (VH) and CH1 constant domain of IgG heavy chain molecule. This Fd molecule was solubilized using guanidine salt and then expressed in the form of inclusion body and successfully refolded into functional antibody molecule by rapid dilution in refolding buffer. B7 Fd reacted with d epitope of hepatitis B virus surface antigen (HBsAg). Its affinity was determined by competition enzyme-linked immunosorbent assay (competition ELISA). The K value of B7 Fd was 3.3 * 10.
