Human lung lavage proteins were fractionated by centrifuganon and molecular sieving. An antiserum to the post-albumin fraction of the soluble proteins reacted with a 10 KD protein and this protein was isolated by conventional chromatography. The protein, which has a p1 of 4.8, consists of two 5 KD polypeptides and is rich in glutamic acid, leucine, 5crme, and aspartic acid amino acids. The protein does not bind to concanavalin A, pancreatic elastase, leukocyte elastase, or trypsin, and lacks anti-protease activity. It constitutes about 0.15% of the soluble proteins in lung lavage. Antibodies to the 10 KD protein specifically and exclusively stain Clara cells in human, dog, and rat. Staining of granules of Clara

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In June 1988, during the grass-pollen season in Leiden, The Netherlands, outdoor airborne particulate matter was collected and separated into fractions according to aerodynamic sizes (greater than or equal to 10 microns, 4.9-10 microns, 2.7-4.9 microns, 1.3-2.7 microns, 0.6-1.3 microns, less than or equal to 0.6 microns), with a cascade impactor mounted on top of a high volume sampler. The different fractions were tested for the presence of grass-pollen allergenic activity using a RAST-inhibition assay: specific IgE-antibody-containing patient serum was applied on the particle-loaded impaction strips, and the serum was recovered by descending elution for further analysis in the RAST. Simultaneously, continuous measurements were made of the airborne grass-pollen concentration using a volumetric pollen trap. Sampling observations lasting 7-9 hr during a period with relatively high airborne grass-pollen concentrations showed reliably detectable amounts of grass-pollen allergen, not only in the first impaction stage where intact pollen were collected, but also in the lower stages collecting the smaller, paucimicronic and submicron atmospheric aerosol fraction. It is evident that this result has serious implications for the understanding of the bronchial symptoms frequently seen in hay fever patients on days with high pollen concentrations in the air.

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The anti-elastase composition of bronchoalveolar lavage (BAL) fluid from alpha 1-proteinase inhibitor (alpha 1PI) deficient and bronchitic patients was determined by immunological and functional assays, together with the cell profile of the BAL fluid. alpha 1PI, anti-leucoprotease and alpha 2-macroglobulin were present in all the samples BAL fluid alpha 1PI concentrations were significantly lower in the group with serum alpha 1PI deficiency. Lavage fluid from alpha 1PI deficient subjects inhibited less porcine pancreatic elastase than bronchitic BAL fluid (P less than 0.005). However, the alpha 1PI was only about 50% active as an inhibitor in both groups. There was no difference in the amount of neutrophil elastase (NE) inhibited per ml of lavage fluid or per mol of the measured inhibitors in the secretions, but both groups inhibited more enzyme than would be expected for these inhibitors (alpha 1PI deficient: median 4.78 mol of NE/mol of known inhibitors, range 0.88-78.80; bronchitic: 1.14, 0.21-4.66), suggesting that an additional inhibitor is present. The total leucocyte and neutrophil counts were elevated (2P less than 0.01) in the lavages of alpha 1PI deficient patients, suggesting a greater potential elastase burden than subjects with normal alpha 1PI.