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.
Article
em Zh
| WPRIM
| ID: wpr-434051
Biblioteca responsável:
WPRO
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.
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WPRIM
Idioma:
Zh
Revista:
Journal of China Pharmaceutical University
Ano de publicação:
2005
Tipo de documento:
Article