EXPRESSION IN ESCHERICHIA-COLI AND PURIFICATION OF SOLUBLE FORMS OF THE F-PROTEIN OF BOVINE RESPIRATORY SYNCYTIAL VIRUS

Authors
NAVAL J PINOL J REBORDOSA X SERRAHARTMANN X PEREZPONS JA QUEROL E
Citation
J. Naval et al., EXPRESSION IN ESCHERICHIA-COLI AND PURIFICATION OF SOLUBLE FORMS OF THE F-PROTEIN OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, Protein expression and purification, 9(2), 1997, pp. 288-294
Citations number
36
Categorie Soggetti
Biology,"Biochemical Research Methods
Journal title
Protein expression and purification → ACNP
ISSN journal
10465928
Volume
9
Issue
2
Year of publication
1997
Pages
288 - 294
Database
ISI
SICI code
1046-5928(1997)9:2<288:EIEAPO>2.0.ZU;2-L
Abstract
Six fragments of the F gene from bovine respiratory syncytial virus (B RSV) were engineered into the pMAL-c2 Escherichia coli expression vect or and expressed as C-terminal maltose-binding protein (MBP) fusion pr oducts. The resulting polypeptides were partially soluble and single-s tep purified by affinity chromatography. These fusion proteins were re cognized in Western blots by several MAbs directed against human respi ratory syncytial virus F protein. In addition, rabbit polyclonal antis era raised against two purified MBP-derived proteins reacted with the BRSV-F protein. (C) 1997 Academic Press.