Purification and characterization of alpha 1-antichymotrypsin from human pleural fluid and human serum.
Human alpha 1-antichymotrypsin was purified from human pleural fluid and from human serum. Four affinity chromatographic steps were required to obtain pure alpha 1-antichymotrypsin.  Pleural and serum alpha 1-antichymotrypsin have the same molecular weight, which was estimated by SDS-polyacrylamide gel electrophoresis to be 58 000. The chemical composition of the two types of alpha 1-antichymotrypsin is the same. Using a technique for visualization of the chymotrypsin inhibitors, we showed that the pure alpha 1-antichymotrypsin obtained from the two physiological fluids had its inhibitory capacity preserved.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D006801:Humans; D008970:Molecular Weight; D010996:Pleural Effusion / Q000032:analysis*; D000514:alpha 1-Antichymotrypsin
D000596:Amino Acids; D002241:Carbohydrates; D000514:alpha 1-Antichymotrypsin; D002918:Chymotrypsin