Production and secretion of recombinant proteins in Dictyostelium discoideum.
Biotechnology (N Y)
; 12(6): 614-8, 1994 Jun.
Article
en En
| MEDLINE
| ID: mdl-7764951
ABSTRACT
We have expressed useful amounts of three recombinant proteins in a new eukaryotic host/vector system. The cellular slime mold Dictyostelium discoideum efficiently secreted two recombinant products, a soluble form of the normally cell surface associated D. discoideum glycoprotein (PsA) and the heterologous protein glutathione-S-transferase (GST) from Schistosoma japonicum, while the enzyme beta-glucuronidase (GUS) from Escherichia coli was cell associated. Up to 20mg/l of recombinant PsA and 1mg/l of GST were obtained after purification from a standard, peptone based growth medium. The secretion signal peptide was correctly cleaved from the recombinant GST- and PsA-proteins and the expression of recombinant PsA was shown to be stable for at least one hundred generations in the absence of selection.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Proteínas Recombinantes
/
Clonación Molecular
/
Proteínas del Complejo del Centro de Reacción Fotosintética
/
Complejo de Proteína del Fotosistema I
/
Dictyostelium
/
Glutatión Transferasa
Límite:
Animals
Idioma:
En
Año:
1994
Tipo del documento:
Article