title: Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli.
abstract: Recombinant single-chain urokinase (rUK1) has been purified from Escherichia coli. The purification utilizes a refractile body purification, followed by batch DE-52 cellulose extraction, hydroxylapatite chromatography, and S-200 chromatography. Two-chain rUK (rUK2) is separated from rUK1 on benzamidine--Sepharose. The purification eliminates proteases early in the procedure so the rUK1 will not be cleaved to rUK2. The rUK1 has been characterized by amino-terminal analysis as well as carboxy-terminal analysis after cleavage by plasmin.
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000302:isolation & purification*; D014568:Urokinase-Type Plasminogen Activator / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D014568:Urokinase-Type Plasminogen Activator