of the recombinant enzyme, using an affinity purification procedure based on the use of a histidine tag in the N terminus of the protein disulfide-isomerase/beta polypeptide
partial, using ammonium sulfate precipitation, column chromatography on DEAE-Sephadex A-50 and affinity chromatography on agarose-linked poly(L-proline) column
partial, using ion-exchange chromatography on DEAE-cellulose, affinity chromatography with poly-L-proline coupled to tresyl-activated Sepharose-4B and gel filtration
separation of the enzyme from the inactive precursor of the enzyme, using ammonium sulfate precipitation and column chromatography on DEAE-Sephadex A-50 and Agarose A-1.5m columns
using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration
using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration
using ammonium sulfate fractionation, affinity chromatography on poly(L-proline) coupled to Sepharose 4B, DEAE-cellulose chromatography, and gel filtration
using ammonium sulfate fractionation, fractionation with calcium phosphate gel, fractionation with alumina gel, chromatography on DEAE-Sephadex and polyacrylamide gel filtration
using ammonium sulfate precipitation, calcium phosphate batch fractionations and anion exchange chromatography on DEAE-agarose followed by gel filtration on agarose
using chromatography on DEAE-Sepharose Fast flow column, ammonium sulfate precipitation, chromatography on phenyl-Superose column, second ammonium sulfate precipitation and column chromatography on Superdex G75 HR
using ion-exchange chromatography on DEAE-cellulose, and affinity chromatography on poly(L-hydroxyproline), 3,4-dihydroxyphenylacetate or 3,4-dihydroxyphenylpropionate linked to Sepharose
using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration
using affinity chromatography on a column containing a polypeptide substrate of the enzyme linked to agarose, elution of the enzyme with a second peptide substrate and separation of the enzyme from this peptide by gel filtration
using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration
using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration
using affinity chromatography on a column containing poly-(L-proline) linked to agarose, elution with the same polypeptide of a lower molecular weight, and gel filtration
using ammonium sulfate fractionation, affinity chromatography on poly(L-proline) coupled to Sepharose 4B, DEAE-cellulose chromatography, and gel filtration
using ammonium sulfate fractionation, affinity chromatography on poly(L-proline) coupled to Sepharose 4B, DEAE-cellulose chromatography, and gel filtration