title: Purification and characterization of canine alpha-1-antiproteinase.
abstract: The principal canine plasma protease inhibitor, alpha-1-antiproteinase, has been purified 90-fold with a 25% yield to apparent homogeneity. The purification scheme includes anion-exchange chromatography, to separate away the bulk of the serum albumin; affinity chromatography by insolubilized concanavalin A, to remove most of the other serum proteins as well as traces of albumin; and, finally, sizing on Sephacryl-S-200. Unique to this purification scheme is the batch use of insolubilized hemoglobin--Sepharose beads to remove the ubiquitous contaminant haptoglobin. The purified material has an apparent molecular weight of 58 000, 11.2% carbohydrate, and an E280nm1% = 5.82, and can be separated by isoelectric focusing into at least two distinct forms with pI values of 4.40 and 4.52. In addition, canine alpha-1-antiproteinase is immunologically distinct from human alpha-1-antiproteinase.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004285:Dogs; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D011480:Protease Inhibitors / Q000097:blood* / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D011480:Protease Inhibitors