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GENE ENGINEERING ARGININE DEIMINASE REFORMED THROUGH SITE DIRECTED MUTAGENESIS
GENE ENGINEERING ARGININE DEIMINASE REFORMED THROUGH SITE DIRECTED MUTAGENESIS
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机译:通过现场定向诱变改造基因工程精氨酸脱氨酶
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摘要
A strain of gene engineering arginine deiminase reformed through site directed mutagenesis, relating to the technical field of gene engineering. The amino acid sequence is SEQ ID No.1, and the 264 site glycine in the amino acid sequence of the arginine deiminase reformed through site directed mutagenesis mutates into proline relative to the amino acid sequence of the natural arginine deiminase. Compared to a wild enzyme, the effective pH action range of the mutant arginine deiminease is expanded to a certain degree, and in particularly, the mutant arginine deiminease has good enzyme activity at the physiological pH value of 7.4. The mutant enzyme has the high stability under the pH value of 5.5-7.5 along with the broadening of the effective pH action range. Therefore, the problems of low enzyme activity and short half-life in vivo under physiological conditions of the clinical applications of the arginine deiminase in tumor treatment are solved, and good conditions are created for the application of the arginine deiminase and the coding gene thereof in clinical treatment.
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机译:通过定点诱变改造的基因工程精氨酸脱亚氨酶菌株,涉及基因工程技术领域。氨基酸序列为SEQ ID No.1,并且通过定点诱变重整的精氨酸脱亚氨酶的氨基酸序列中的264位甘氨酸相对于天然精氨酸脱亚氨酶的氨基酸序列突变成脯氨酸。与野生酶相比,突变型精氨酸脱亚胺酶的有效pH作用范围扩大到一定程度,特别是突变型精氨酸脱亚胺酶在7.4的生理pH值下具有良好的酶活性。突变型酶在5.5-7.5的pH值下具有较高的稳定性,并且有效pH作用范围的扩大。因此,解决了精氨酸脱亚氨酶在肿瘤治疗中的临床应用在生理条件下体内酶活性低,半衰期短的问题,为精氨酸脱亚氨酶及其编码基因的应用创造了良好的条件。临床治疗。
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