title: Affinity chromatography of alpha-1-protease inhibitor using Sepharose-4B-bound anhydrochymotrypsin.
abstract: Sepharose 4B-bound bovine anhydrochymotrypsin (AnhCT), a catalytically inactive form of chymotrypsin, was shown to be effective for retaining active alpha-1-protease inhibitor (alpha-1-PI, also alpha-1-antitrypsin) from human plasma, while showing no measurable affinity for oxidized or protease complexed alpha-1-PI, or for most other plasma proteins. alpha-1-PI eluted from this resin with 0.1 M chymostatin retained full activity against trypsin, chymotrypsin, and elastase. In addition to alpha-1-PI, AnhCT-Sepharose binds a limited number of other plasma proteins. Using monospecific antisera to plasma protease inhibitors, one of these proteins was identified as inter-alpha-trypsin inhibitor, and it was recoverable in active form. Therefore, an AnhCT-Sepharose 4B resin has been demonstrated to be of value for isolating active forms of alpha-1-PI from solutions, and may also be useful for the isolation of inter-alpha-trypsin inhibitor.
mesh_terms: D001798:Blood Proteins; D002384:Catalysis; D002846:Chromatography, Affinity; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D012116:Resins, Plant; D012685:Sepharose; D000515:alpha 1-Antitrypsin
chemical_list: D001798:Blood Proteins; D012116:Resins, Plant; D000515:alpha 1-Antitrypsin; D012685:Sepharose; D002918:Chymotrypsin; C000653:anhydrochymotrypsin