Shub D A, Casna N J
Gene. 1985;37(1-3):31-6. doi: 10.1016/0378-1119(85)90254-9.
The amino-terminal portion of the T4 rIIB gene has been fused to the coding sequence of a truncated lacZ gene from Escherichia coli, giving rise to a fusion protein with beta-galactosidase activity. The 3192-bp rIIB-lacZ gene fusion was transferred into phage T4, and enzymatically active protein was produced after phage infection. T4 may be a useful expression vector in special circumstances, in particular for proteins whose accumulation in E. coli is limited by sensitivity to proteases.
T4 rIIB基因的氨基末端部分已与来自大肠杆菌的截短型lacZ基因的编码序列融合，产生了具有β-半乳糖苷酶活性的融合蛋白。将3192bp的rIIB-lacZ基因融合体转入噬菌体T4，噬菌体感染后产生了具有酶活性的蛋白。在特殊情况下，T4可能是一种有用的表达载体，特别是对于那些在大肠杆菌中因对蛋白酶敏感而积累受限的蛋白质。
