TY - JOUR
T1 - Expression in Escherichia coli and purification of soluble forms of the F protein of bovine respiratory syncytial virus
AU - Naval, Jordi
AU - Piñol, Jaume
AU - Rebordosa, Xavier
AU - Serra-Hartmann, Xavier
AU - Pérez-Pons, Josep A.
AU - Querol, Enrique
PY - 1997/1/1
Y1 - 1997/1/1
N2 - Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2 Escherichia coli expression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affinity chromatography. These fusion proteins were recognized in Western blots by several MAbs directed against human respiratory syncytial virus F protein. In addition, rabbit polyclonal antisera raised against two purified MBP-derived proteins reacted with the BRSV-F protein.
AB - Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2 Escherichia coli expression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affinity chromatography. These fusion proteins were recognized in Western blots by several MAbs directed against human respiratory syncytial virus F protein. In addition, rabbit polyclonal antisera raised against two purified MBP-derived proteins reacted with the BRSV-F protein.
U2 - https://doi.org/10.1006/prep.1996.0688
DO - https://doi.org/10.1006/prep.1996.0688
M3 - Article
VL - 9
SP - 288
EP - 294
ER -