[Fusion and expression of the gene encoding human Mn-SOD to anti-CEA single-chain antibody in Escherichia coli].
The gene encoding human manganese-superoxide dismutase (Mn-SOD) was fused to anti-carcinoembryonic antigen single-chain antibody gene to construct the fusion gene, then was ligated into prokaryotic expression vector pET-22b(+), The fusion gene was expressed in E. coli at high level, accounting for 24% of the total bacteria soluble protein; and was characterized by SDS-PAGE and Western-blot analysis; the expression product had the CEA-binding ability in RIA, and also had the SOD activity by pyrogallol autoxidation assay. So, the Mn-SOD moiety retains substantial enzymatic activity, where the ScFv moiety can deliver the fusion protein to tumor, Mn-SOD is a potential tumor-suppressor gene, maybe the fusion protein can provide a new pathway to tumor therapy.
He
H J
HJ
Institute of Biochemistry, East China University of Science and Technology, Shanghai 200237.
Yang
W D
WD
Chang
Y N
YN
Shi
H J
HJ
Yang
G Z
GZ
Wu
X F
XF
Yuan
Q S
QS
D000595:Amino Acid Sequence; D001483:Base Sequence; D002272:Carcinoembryonic Antigen / Q000276:immunology*; D004926:Escherichia coli / Q000235:genetics*; D006801:Humans; D007128:Immunoglobulin Fragments / Q000235:genetics*; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*; D013482:Superoxide Dismutase / Q000235:genetics*
D002272:Carcinoembryonic Antigen; D007128:Immunoglobulin Fragments; D011993:Recombinant Fusion Proteins; C055966:immunoglobulin Fv; D013482:Superoxide Dismutase