title: Expression and purification of the recombinant mustard trypsin inhibitor 2 (MTI2) in Escherichia coli.
abstract: 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.
authors.affiliation: Department of Industrial Chemistry, University of Bologna, Italy.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Stefan
authors.forename: Luisa
authors.initials: L
authors.lastname: Ugolini
authors.forename: Elena
authors.initials: E
authors.lastname: Martelli
authors.forename: Sandro
authors.initials: S
authors.lastname: Palmieri
authors.forename: Alejandro
authors.initials: A
authors.lastname: Hochkoeppler
mesh_terms: 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
chemical_list: C405940:MTI2 protein, Sinapis alba; D010940:Plant Proteins; D011994:Recombinant Proteins