12 % SDS-PAGE gel of protein extracts from E. coli BL21(DE3) cells transformed with different pET-16b expression plasmids as indicated above the gel lanes. Note the strong 45 and 55 kDa bands in the IPTG-induced samples of BL21(DE3) carrying pET-16bcfa and pET16bcfs1, respectively. Protein extracts (30 μl each) were from non-induced (-IPTG; left) and ITPGinduced cultures (+ IPTG, right).

Contexts in source publication

Context 1

... identification after expression in E. coli B strain BL21(DE3).Vector-transformed E. coli BL21(DE3) clones were cultivated for protein isolation as described in the methods. Aliquots of all protein samples were separated by SDS-PAGE and stained by Coomassie (Fig. 2). Intensities of most protein bands in the gel were comparable between the different probes, including in the samples of clones that were transformed with the antisense constructs. In the samples with the sense-plasmids pET-16bcfa and pET-16bcfs1 however, stronger blue bands were clearly visible at gel positions of around 45 kDa and 55 ...

Context 2

... pET-16bcfa and pET-16bcfs1 however, stronger blue bands were clearly visible at gel positions of around 45 kDa and 55 kDa, respectively. A slightly stronger band of corresponding size was also detectable by eye in the IPTG-non-induced sample of BL21(DE3) with the pET-16bcfa plasmid but not in the sample of BL21(DE3) with the pET-16bcfs1 plasmid (Fig. 2). The theoretical masses of the native E. coli protein Cfa and the native C. cinerea protein Cfs1 corresponded roughly to the size of the two strong bands seen in Fig. 2 in the sense-vector samples induced by IPTG. The fusion proteins produced recombinantly from the pET-16b vector should, however, be slightly larger than the native ...

Context 3

... size was also detectable by eye in the IPTG-non-induced sample of BL21(DE3) with the pET-16bcfa plasmid but not in the sample of BL21(DE3) with the pET-16bcfs1 plasmid (Fig. 2). The theoretical masses of the native E. coli protein Cfa and the native C. cinerea protein Cfs1 corresponded roughly to the size of the two strong bands seen in Fig. 2 in the sense-vector samples induced by IPTG. The fusion proteins produced recombinantly from the pET-16b vector should, however, be slightly larger than the native proteins by the extra 3.21 kDa obtained through the Nterminal addition of the artificial sequence MGHHHHHHHHHHSSFHIEGRHMLEDP (see Fig. ...