Puohiniemi R, Butcher S, Tarkka E, Sarvas M
National Public Health Institute, Helsinki, Finland.
FEMS Microbiol Lett. 1991 Sep 15;67(1):29-33. doi: 10.1016/0378-1097(91)90438-g.
A high yield of Escherichia coli outer membrane proteins OmpA (about 200 mg/l) and OmpF (about 100 mg/l) was obtained in Bacillus subtilis when produced intracellularly. The yield was more than 100-fold higher than the yield of these proteins by a similar vector containing the complete signal sequence of alpha-amylase of B. amyloliquefaciens. Both proteins isolated after breakage of the B. subtilis cells by low-speed centrifugation were about 70% pure and could be solubilized by Sarkosyl, SDS and guanidine hydrochloride.
当在枯草芽孢杆菌中进行胞内表达时，可获得高产的大肠杆菌外膜蛋白OmpA（约200 mg/l）和OmpF（约100 mg/l）。与含有解淀粉芽孢杆菌α-淀粉酶完整信号序列的类似载体相比，这些蛋白的产量提高了100倍以上。通过低速离心破碎枯草芽孢杆菌细胞后分离得到的这两种蛋白纯度约为70%，并且可被十二烷基肌氨酸钠、十二烷基硫酸钠和盐酸胍溶解。
