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Effect of N0terminal deletions on the activity of pokeweed antiviral protein expressed in E.coli

机译:N0末端缺失对大肠杆菌表达的商陆抗病毒蛋白活性的影响

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摘要

Pokeweed antiviral protein(PAP) from Phytolacca americana is a highly specific N0glycosidase removing adenine residues(A~4324 in 28S rRNA and A~2660in 23S rRNA) from intact ribosomes of both eukaryotes and prokaryotes. Due to the ribosome impairing activity the gene coding for mature PAP has not been expressed so far in bacteria whereas the full-length gene(coding for the mature 262 amino acids plus two signal peptides of 22 and 29 amino acids at both N- and C-termini, respectively) has been expressed in Escherichia coli.
机译:美洲疫霉的商陆抗病毒蛋白(PAP)是一种高度特异性的N0糖苷酶,可去除真核生物和原核生物完整核糖体中的腺嘌呤残基(28S rRNA中的A〜4324和23S rRNA中的A〜2660)。由于核糖体活性受损,迄今为止尚未在细菌中表达编码成熟PAP的基因,而全长基因(编码成熟的262个氨基酸以及N和C处的22和29个氨基酸的两个信号肽) -末端)已在大肠杆菌中表达。

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