Abstract
Three major antiprotease components in equine serum were identified and characterized. These were the acidic prealbumin Pr, the homolog of human alpha-1 antitrypsin and 2 protease binding proteins, the acidic prealbumin Xc and alpha-2 macroglobulin, both capable of inhibiting the proteolytic activity of trypsin, but with only limited inhibitory effect on its esterolytic activity. The possible role of these serum antiproteases in the onset of chronic obstructive pulmonary disease (COPD), analogous to the hereditary dysproteinemia of alpha-1 antitrypsin in man, was investigated. There was no evidence of a genetically determined variation in the protease binding proteins, but an increased frequency of the electrophoretically slower Pr antitrypsin alleles was present in horses with COPD. The mixed breeding of the animals investigated and the lack of correlation with low serum trypsin inhibitory capacity, measured by inhibition of DL-BAPA [benzoyl-DL-arginine-P-nitroanilide] hydrolysis, clouded the significance of this observation.