Abstract
Abstract
The interactions of a partially purified elastase inhibitor from bovine pulmonary macrophages were investigated using pancreatic elastase. The inhibitor was prepared from lysed pulmonary macrophages obtained by lavage of excised bovine lung lobes. In the presence of pancreatic elastase, the inhibitor formed a stable complex. Complex formation did not occur, however, if the elastase was first inactivated by pretreatment with phenylmethylsulfonyl fluoride. Fractions containing inhibitory activity were recovered from calibrated columns of Sephadex G-100 or G-150 in the molecular weight range of 40,000–50,000. Following incubation of the inhibitor with elastase, the inhibitor-elastase complex eluted in the molecular weight range of 65,000–75,000, suggesting a 1:1 molar ratio of inhibitor to elastase. The partially purified inhibitor did not inhibit trypsin, indicating that the bovine macrophage inhibitor did not arise from endocytosis of α-1-protease inhibitor.
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