title: Human alpha-1-antichymotrypsin: purification and properties.
abstract: Human alpha-1-antichymotrypsin has been purified to homogeneity by the following sequential steps--(a) ammonium sulfate fractionation; (b) chromatography on Cibacron Blue Sepharose at pH 7.0; and (c) chromatography on SP-Sephadex C-50 at pH 5.5. The inhibitor has a molecular weight near 68,000 and contains approximately 26% carbohydrate alpha-1-Antichymotrypsin has an amino-terminal arginine and a carboxy-terminal glycine. It also has some homology with alpha-1-PI based on amino-terminal sequence analysis of both proteins. Complexes of alpha-1-antichymotrypsin with human chymotrypsin and human leukocyte cathepsin G are stable in sodium dodecyl sulfate and have molecular weights near 90,000 suggesting 1:1 complex formation on a molar basis between inhibitor and enzyme.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006023:Glycoproteins / Q000097:blood / Q000302:isolation & purification / Q000494:pharmacology; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000097:blood* / Q000302:isolation & purification / Q000494:pharmacology
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D011480:Protease Inhibitors; D002918:Chymotrypsin