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( Zu Yong He ),( Yuankai Huang ),( Yufeng Qin ),( Zhiguo Liu ),( Delin Mo ),( Peiqing Cong ),( Yaosheng Chen ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.4
The secretory efficiency of recombinant xylanase xynB from yeast Pichia pastoris between the α-factor preprosequence and a classical mammalian signal peptide derived from bovine β-casein was compared. The results showed that although the bovine β-casein signal peptide could direct highlevel secretion of recombinant xylanase, it was relatively less efficient than the α-factor preprosequence. In contrast, the bovine β-casein signal peptide caused remarkably more recombinant xylanase trapped intracellularly. Realtime RT-PCR analysis indicated that the difference in the secretory level between the two signal sequences was not due to the difference in the transcriptional efficiency.