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Construction and Enzyme-activity Assessment of L-Asparaginase Mutants / 中国药科大学学报
Journal of China Pharmaceutical University ; (6): 468-472, 2005.
Artículo en Chino | WPRIM | ID: wpr-434051
ABSTRACT

AIM:

To construct nine novel L-asparaginase mutants and study their enzyme-activity.

METHODS:

The mutants were constructed using overlap extension PCR according to the principle of alanine-scanning mutagenesis. The enzyme-activity was detected by Nessler's method.

RESULTS:

The DNA sequencing showed that the mutagenesis was consistent with the theoretical prediction. The enzyme-activity assay demonstrated that each mutant possessed enzyme activity equal to the original enzyme.

CONCLUSION:

Through gene modification,epitop of L-asparaginase was changed without activity loss.These results provide foundation for further study of the structure-function relationship of L-asparaginase.

Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Journal of China Pharmaceutical University Año: 2005 Tipo del documento: Artículo

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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Journal of China Pharmaceutical University Año: 2005 Tipo del documento: Artículo