Structural requirements for bacterial expression of stable, enzymatically active fusion proteins containing the human immunodeficiency virus reverse transcriptase.
DNA
; 7(6): 407-16, 1988.
Article
em En
| MEDLINE
| ID: mdl-2462482
ABSTRACT
A collection of variant plasmids that express the human immunodeficiency virus (HIV) reverse transcriptase as trpE fusion proteins were generated and scored for their ability to produce stable, active proteins. Trimming portions of the viral pol gene resulted in dramatic increases in yield over earlier constructs; the accumulation of high levels of enzymatically active protein in this system was increased by the retention of the trpE sequences at the amino terminus. A new in situ gel activity assay was used to demonstrate that the major induced protein, containing approximately 68 kD of viral sequences, was the active species.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes de Fusão
/
Proteínas Recombinantes
/
HIV
/
DNA Polimerase Dirigida por RNA
/
Escherichia coli
/
Genes
/
Genes Virais
Idioma:
En
Ano de publicação:
1988
Tipo de documento:
Article