The Preparation of the Antigen Conformation-related Monoclonal Antibodies against Maltose-Binding Protein.
Making use of the high expression efficiency of maltose-binding protein (MBP) in E. coli, the soluble and the inclusion body forms of MBP were purified to homogeneity by affinity chromatography and by denaturation, refolding and gel filtration respectively. After immunized Balb/C mice with two forms of MBP respectively, 5 clones for each antigen form were found to secrete monoclonal antibodies. The binding experiments showed that two antibodies obtained by the immunization with the refolded form of MBP had high affinity to the denatured MBP.
Xiong
Shun-Bin
SB
Shanghai Institute of Biochemistry, the Chinese Academy of Sciences, Shanghai 200031, China.
Ding
Jian-Fang
JF
Wang
Wei-Qin
WQ
Li
Lin
L
Xu
Gen-Jun
GJ