Wang Haikuan, Zhao Xinhuai, Lu Fuping
Key Lab of Diary Science, Ministry of Education, Harbin, PO 150030, P. R. China.
Biochemistry (Mosc). 2007 Jun;72(6):640-3. doi: 10.1134/s0006297907060065.
According to the bias of codon utilization of Pichia methanolica, a fragment encoding bovine lactoferricin has been cloned and expressed in the P. methanolica under the control of the alcohol oxidase promoter, which was followed by the Saccharomyces cerevisiae alpha-factor signal peptide. The alpha-factor signal peptide efficiently directed the secretion of bovine lactoferricin from the recombinant yeast cell. The recombinant bovine lactoferricin appears to be successfully expressed, as it displays antibacterial activity (antibacterial assay). Moreover, the identity of the recombinant product was estimated by Tricine-SDS-PAGE.
根据甲醇毕赤酵母密码子使用偏好，一个编码牛乳铁蛋白肽的片段已被克隆，并在甲醇氧化酶启动子控制下在甲醇毕赤酵母中表达，该启动子后接酿酒酵母α-因子信号肽。α-因子信号肽有效地引导重组酵母细胞分泌牛乳铁蛋白肽。重组牛乳铁蛋白肽似乎成功表达，因为它表现出抗菌活性（抗菌试验）。此外，通过Tricine-SDS-PAGE对重组产物进行了鉴定。
