Expression and purification of the recombinant mustard trypsin inhibitor 2 (MTI2) in Escherichia coli.
The mustard trypsin inhibitor 2, MTI2, was expressed in Escherichia coli. A specific procedure for its production and purification is described. The recombinant protein was recovered by protein extraction from the insoluble fraction, then renatured and purified by ion exchange and gel filtration chromatography. Finally, the inhibitory activity against trypsin was also determined.
Stefan
Alessandra
A
Department of Industrial Chemistry, University of Bologna, Italy.
Ugolini
Luisa
L
Martelli
Elena
E
Palmieri
Sandro
S
Hochkoeppler
Alejandro
A
D001483:Base Sequence; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D009149:Mustard Plant / Q000235:genetics / Q000502:physiology; D010940:Plant Proteins / Q000235:genetics* / Q000302:isolation & purification; D020673:Protein Renaturation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D015183:Restriction Mapping; D012639:Seeds / Q000502:physiology; D012995:Solubility
C405940:MTI2 protein, Sinapis alba; D010940:Plant Proteins; D011994:Recombinant Proteins