Purification and characterization of human bronchial proteinase inhibitor.
We describe a purification procedure for the human bronchial proteinase inhibitor which involves trichloroacetic acid precipitation of sputum followed by ion-exchange and gel filtration chromatography. The inhibitor shows a major band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but exhibits microheterogeneity on high-resolution chromatography. It has a molecular mass of 15.5-16 kDa as determined by electrophoresis and gel filtration and is 90% active against leukocyte elastase. The amino acid sequence of the N-terminal portion of the inhibitor was determined and was found to be identical (through 29 amino acids) to that recently reported for the human seminal plasma proteinase inhibitor I (Seemuller et al. (1986) FEBS Lett. 199, 43-48).
D000595:Amino Acid Sequence; D001980:Bronchi / Q000032:analysis*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D008297:Male; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000097:blood; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification*; D012661:Semen / Q000032:analysis; D015843:Serpins; D013183:Sputum / Q000032:analysis
D011480:Protease Inhibitors; D011506:Proteins; D015843:Serpins; D010196:Pancreatic Elastase