Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris.
FEBS Lett
; 468(2-3): 137-41, 2000 Feb 25.
Article
en En
| MEDLINE
| ID: mdl-10692574
ABSTRACT
The mustard trypsin inhibitor MTI2 was expressed as secretory protein in the yeast Pichia pastoris. In order to evaluate the influence of the C-terminal amino acids of the precursor form on the inhibitor activity, the C-terminal precursor and the mature protein were both expressed. A third His-tagged construct was also designed to compare alternative purification procedures. Proteins were efficiently expressed at levels of 40-160 mg/l in shake flasks. Equilibrium dissociation constants demonstrated that the mature protein was a stronger inhibitor of bovine beta-trypsin compared to the precursor and His-tagged forms (0.01 nM vs. 0.58 nM and 0.71 nM, respectively). The recombinant proteins were active inhibitors of Spodoptera exigua gut proteases.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Plantas Medicinales
/
Tripsina
/
Inhibidores de Tripsina
/
Planta de la Mostaza
Límite:
Animals
Idioma:
En
Año:
2000
Tipo del documento:
Article