Mutant recombinant reverse transcriptase as well as preparation method and application thereof
The invention discloses a mutant recombinant reverse transcriptase as well as a preparation method and application thereof. The specific mutation sites are as follows: the 67th amino acid of a wild reverse transcriptase M-MLV is mutated from S to T, the 303th amino acid is mutated from F to R, the 3...
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| creator | JIA PEIYAO YU WEI YOU QIMIN ZHAN HAO ZHOU YANQIONG LIN YIZHI WANG XINCHAO WANG BINGNAN SHUAI JINXIAO YANG QIWEN ZHU YING LIN YUANKUI |
| description | The invention discloses a mutant recombinant reverse transcriptase as well as a preparation method and application thereof. The specific mutation sites are as follows: the 67th amino acid of a wild reverse transcriptase M-MLV is mutated from S to T, the 303th amino acid is mutated from F to R, the 312th amino acid is mutated from L to S, the 432nd amino acid is mutated from L to G, the 479th amino acid is mutated from N to F, and the 524th amino acid is mutated from D to Q. The transcriptase is obtained through IPTG induced expression by artificially synthesizing an expression vector and utilizing a preferred host cell. The activity temperature of the modified recombinant mutant reverse transcriptase is 37-65 DEG C, the reverse transcription efficiency of the modified recombinant mutant reverse transcriptase is 41.9 times that of a wild reverse transcriptase, and the endurance capacity of the modified recombinant mutant reverse transcriptase to common interferents is obviously improved. The performance of the |
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The specific mutation sites are as follows: the 67th amino acid of a wild reverse transcriptase M-MLV is mutated from S to T, the 303th amino acid is mutated from F to R, the 312th amino acid is mutated from L to S, the 432nd amino acid is mutated from L to G, the 479th amino acid is mutated from N to F, and the 524th amino acid is mutated from D to Q. The transcriptase is obtained through IPTG induced expression by artificially synthesizing an expression vector and utilizing a preferred host cell. The activity temperature of the modified recombinant mutant reverse transcriptase is 37-65 DEG C, the reverse transcription efficiency of the modified recombinant mutant reverse transcriptase is 41.9 times that of a wild reverse transcriptase, and the endurance capacity of the modified recombinant mutant reverse transcriptase to common interferents is obviously improved. 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The specific mutation sites are as follows: the 67th amino acid of a wild reverse transcriptase M-MLV is mutated from S to T, the 303th amino acid is mutated from F to R, the 312th amino acid is mutated from L to S, the 432nd amino acid is mutated from L to G, the 479th amino acid is mutated from N to F, and the 524th amino acid is mutated from D to Q. The transcriptase is obtained through IPTG induced expression by artificially synthesizing an expression vector and utilizing a preferred host cell. The activity temperature of the modified recombinant mutant reverse transcriptase is 37-65 DEG C, the reverse transcription efficiency of the modified recombinant mutant reverse transcriptase is 41.9 times that of a wild reverse transcriptase, and the endurance capacity of the modified recombinant mutant reverse transcriptase to common interferents is obviously improved. 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The specific mutation sites are as follows: the 67th amino acid of a wild reverse transcriptase M-MLV is mutated from S to T, the 303th amino acid is mutated from F to R, the 312th amino acid is mutated from L to S, the 432nd amino acid is mutated from L to G, the 479th amino acid is mutated from N to F, and the 524th amino acid is mutated from D to Q. The transcriptase is obtained through IPTG induced expression by artificially synthesizing an expression vector and utilizing a preferred host cell. The activity temperature of the modified recombinant mutant reverse transcriptase is 37-65 DEG C, the reverse transcription efficiency of the modified recombinant mutant reverse transcriptase is 41.9 times that of a wild reverse transcriptase, and the endurance capacity of the modified recombinant mutant reverse transcriptase to common interferents is obviously improved. The performance of the</abstract><oa>free_for_read</oa></addata></record> |
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| subjects | BEER BIOCHEMISTRY CHEMISTRY COMPOSITIONS OR TEST PAPERS THEREFOR COMPOSITIONS THEREOF CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL ORENZYMOLOGICAL PROCESSES CULTURE MEDIA ENZYMOLOGY MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEICACIDS OR MICROORGANISMS METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING PROCESSES OF PREPARING SUCH COMPOSITIONS PROCESSES USING MICROORGANISMS PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS SPIRITS VINEGAR WINE |
| title | Mutant recombinant reverse transcriptase as well as preparation method and application thereof |
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