title: Qualitative studies of lung lavage alpha 1-proteinase inhibitor.
abstract: A method is described which enables identification of the molecular size of alpha 1-proteinase inhibitor (alpha 1-PI) in biological fluids. This technique when applied to bronchoalveolar lavage fluids clearly demonstrates alpha 1-PI in three molecular forms; the native molecule (Mr approximately equal to ++54 000), a partially proteolysed form (Mr approximately equal to 49 000) and in a form suggestive of a complex with enzyme (Mr approximately equal to 82 000). Samples showing the presence of native alpha 1-PI inhibited more porcine pancreatic elastase than samples where no native alpha 1-PI was seen or where the predominant form was partially proteolysed alpha 1-PI (p less than 0.01). Although the predominant band of alpha 1-PI was more frequently the partially proteolysed form in current smokers (p less than 0.01), there was no clear difference in the inhibitory function of alpha 1-PI between current smokers and non-smokers and those with and without airflow obstruction.
mesh_terms: D000328:Adult; D000368:Aged; D001798:Blood Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006801:Humans; D008168:Lung / Q000032:analysis*; D008173:Lung Diseases, Obstructive / Q000378:metabolism; D008875:Middle Aged; D009504:Neutrophils / Q000201:enzymology; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D012907:Smoking; D007507:Therapeutic Irrigation; D000515:alpha 1-Antitrypsin
chemical_list: D001798:Blood Proteins; D000515:alpha 1-Antitrypsin; D010196:Pancreatic Elastase