ISOLATION AND CHARACTERIZATION OF 2 ALPHA-1-PROTEASE INHIBITORS IN RAT SERUM

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Abstract
On polyacrylamide gels, one .alpha.1-protease inhibitor (R-1) appeared at the leading edge of the albumin, the other (R-2) at the trailing edge. The 2 inhibitors had differing MW, and inhibitory spectra toward protease and were immunologically distinct. The assays for antiprotease activity were performed on whole human and rat sera and inhibitor-enriched fractions of rat serum that was electrophoresed on polyacrylamide gels. The more rapidly migrating antiprotease of rat serum, R-1, inhibited trypsin, chymotrypsin and elastase. The more slowly migrating antiprotease, R-2, inhibited both trypsin and chymotrypsin but possessed only weak anti-elastase activity. When a comparison was made between human .alpha.1-antitrypsin and the more rapidly migrating rat inhibitor, they had similar MW, inhibitory spectra and electrophoretic mobilities. The relevance of the study of the R-1 inhibitor in the pathogenesis of experimental emphysema was emphasized.

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