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Mutations in E154 of Diphtheria Toxin (DT) and Their Biologic Activity / 生物化学与生物物理进展
Progress in Biochemistry and Biophysics ; (12)2006.
Article in Chinese | WPRIM | ID: wpr-586866
ABSTRACT
According to the results of quantum chemistry calculation and the present research status in the relationship between the structures and the functions of DT, the E154 in DT catalyzing domain was mutated to aspartic acid and arginine in order to study the effects of the alteration on the biological activities. By means of gene site-direct mutation, two mutated genes were prepared and the high performance expression was obtained in E.coli system. The results of toxcity studies indicated that the acute toxicity in guinea pig and cytotoxicities of mutant E154D increased slightly in compared with those of recombination wild toxin, and contrarily, those of E154R decreased obviously.

Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Progress in Biochemistry and Biophysics Year: 2006 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Progress in Biochemistry and Biophysics Year: 2006 Type: Article