Efficient production of soluble human beta-defensin-3–4 fusion proteins in Escherichia coli cell-free system

2007 ◽  
Vol 42 (3) ◽  
pp. 423-428 ◽  
Author(s):  
Haiqin Chen ◽  
Limei Fan ◽  
Zhinan Xu ◽  
Xiufei Yin ◽  
Peilin Cen
1983 ◽  
Vol 168 (3) ◽  
pp. 489-503 ◽  
Author(s):  
Rafael P. Mellado ◽  
Kenneth Murray ◽  
P. Chambon

2013 ◽  
Vol 30 (3) ◽  
pp. 893-901 ◽  
Author(s):  
Xu Zhang ◽  
Jiayuan Sheng ◽  
Lei Huang ◽  
Liping Du ◽  
Jin Cai ◽  
...  

1972 ◽  
Vol 128 (3) ◽  
pp. 481-489 ◽  
Author(s):  
J. W. Robinson

The coat protein subunit of the RNA bacteriophage ZIK/1 has a molecular weight of 12100 and does not contain histidine, methionine and cysteine. The amino acid composition of the coat protein is different from that of other RNA bacteriophage coat proteins. Bacteriophage ZIK/1 belongs to a class of RNA bacteriophages distinct from the f2 type, which lack histidine in their coat proteins, and the Qβ type, which lack histidine and methionine. Bacteriophage ZIK/1 RNA is an efficient template in the Escherichia coli cell-free system producing coat protein as the major product and a number of non-coat proteins. This result is similar to that obtained with RNA from f2-type bacteriophages. It is probable that the genomes of RNA bacteriophages are structurally similar and that differences between the types of RNA bacteriophage arise from minor differences in RNA sequence.


1982 ◽  
Vol 60 (12) ◽  
pp. 1095-1100 ◽  
Author(s):  
Yew Phew See ◽  
Bernard R. Glick

An Escherichia coli coupled transcription–translation cell-free system, which is efficient in the synthesis of proteins directed by exogenously added DNA, is described. These cell-free extracts direct protein synthesis against a low background of endogenous protein synthesis providing a means for analyzing the expression of isolated genes. This is especially important when using restriction enzyme-linearized DNAs which are less efficient templates than circular DNAs. This cell-free system has been used to study the expression of the proteins coded by plasmids pBR322 and pBL101.


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