. 2011 Jul-Sep;3(3):77–84.

Table 2.

Efficiency of the method of fusion proteins (TRX-tmFGFR3) and target peptides (tmFGFR3) production

TM-peptide	Molecular weight, kDa	Aminoacid sequence of a TM fragment^a	EK^b, u/mg	Yield^c, mg/ml
TM-peptide	Molecular weight, kDa	Aminoacid sequence of a TM fragment^a	EK^b, u/mg	TRX-tmFGFR3	tmFGFR3
tmFGFR3-nat	4.6	L³⁵⁷PAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLR³⁹⁹	25	40	6
tmFGFR3-R	4.7	L³⁵⁷PAEEELVEADEAGSVYAGILSYR³⁸⁰VGFFLFILVVAAVTLCRLR³⁹⁹	30	20	4
tmFGFR3-E	4.7	L³⁵⁷PAEEELVEADEAGSVYAGILSYGVGFFLFILVVE³⁹¹AVTLCRLR³⁹⁹	30	50	7

The putative TM domains are indicated as gray boxes. The point mutations Gly380Arg (tmFGFR3-R) and Ala391Glu (tmFGFR3-E) appear in bold.

Activity of the enterokinase light chain required to hydrolyze 1 mg of TRX-tmFGFR3 fusion proteins.

The average yield (per 1 L of bacterial culture in M9 minimal media) of the fusion proteins (TRX-tmFGFR3) and purified peptides (tmFGFR3), including their ¹⁵ N- and [ ¹⁵ N-, ¹³ C]-labelled derivatives. The yields were estimated by the intensity of the Coomassie blue-stained bands in SDS-PAGE and by weighing pure, dried tmFGFR3 peptides.