Qualitative studies of lung lavage alpha 1-proteinase inhibitor

Hoppe Seylers Z Physiol Chem. 1984 Apr;365(4):503-10. doi: 10.1515/bchm2.1984.365.1.503.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Blood Proteins / analysis*
  • Chemical Phenomena
  • Chemistry
  • Densitometry
  • Electrophoresis, Polyacrylamide Gel / methods
  • Humans
  • Lung / analysis*
  • Lung Diseases, Obstructive / metabolism
  • Middle Aged
  • Neutrophils / enzymology
  • Pancreatic Elastase / antagonists & inhibitors
  • Smoking
  • Therapeutic Irrigation
  • alpha 1-Antitrypsin


  • Blood Proteins
  • alpha 1-Antitrypsin
  • Pancreatic Elastase