Synthesis of a wheat storage protein subunit in Escherichia coli using novel expression vectors.
Gene
; 35(1-2): 159-67, 1985.
Article
en En
| MEDLINE
| ID: mdl-3928444
ABSTRACT
Useful plasmid expression vectors have been constructed which allow the synthesis of beta-galactosidase (betaG) fusion polypeptides or of polypeptides specified by cDNA clones in Escherichia coli hosts. A foreign DNA fragment can be inserted in any one of the three reading frames at the unique EcoRI, BamHI or SmaI sites immediately after the initiation codon. The cloned foreign gene is under the control of the lac promoter. Using a cDNA clone that encodes part of a wheat storage protein [a high-Mr (HMW) glutenin subunit] synthesis of a glutenin-beta G fusion protein was demonstrated. Synthesis of the glutenin polypeptide, not fused to beta G, was achieved by replacing the lacZYA genes with a stop codon.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Escherichia coli
/
Vectores Genéticos
/
Glútenes
Idioma:
En
Revista:
Gene
Año:
1985
Tipo del documento:
Article