Expression inEscherichia coliand Purification of Soluble Forms of the F Protein of Bovine Respiratory Syncytial Virus

Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2Escherichia coliexpression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affini...

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Published in:Protein expression and purification 1997-03, Vol.9 (2), p.288-294
Main Authors: Naval, Jordi, Piñol, Jaume, Rebordosa, Xavier, Serra-Hartmann, Xavier, Pérez-Pons, Josep A., Querol, Enrique
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cited_by cdi_FETCH-LOGICAL-c1338-4012f5249275036bdd5e07065ee84cc39b156a48ed9fd2de7324ad2675bafa6b3
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container_end_page 294
container_issue 2
container_start_page 288
container_title Protein expression and purification
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creator Naval, Jordi
Piñol, Jaume
Rebordosa, Xavier
Serra-Hartmann, Xavier
Pérez-Pons, Josep A.
Querol, Enrique
description Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2Escherichia coliexpression 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.
doi_str_mv 10.1006/prep.1996.0688
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title Expression inEscherichia coliand Purification of Soluble Forms of the F Protein of Bovine Respiratory Syncytial Virus
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