A peak of immunoreactive pancreatic elastase 2 with a molecular weight consistent with that of a complex of elastase 2 and alpha 1-protease inhibitor (also referred to as alpha 1-antitrypsin) can be detected by radioimmunoassay in normal human serum or plasma (Geokas et al., J. Biol. Chem. 252:61-67, 1977). This material has been purified by gel filtration on Sephadex G-200 and by ion-exchange chromatography on DEAE-cellulose. The alpha 1-protease inhibitor-bound immunoreactive elastase 2 has been dissociated by incubation with hydroxylamine, and the resulting immunoreactive product isolated by gel filtration on Sephadex G-100. The dissociated immunoreactive elastase 2 was shown by affinity chromatography on turkey egg white inhibitor-bound agarose, before and after activation by bovine trypsin, to consist only of proelastase 2. A second peak of immunoreactive material associated with the high molecular weight fraction of plasma has been shown to result from a specific interaction of the 125I-labeled phenylmethanesulfonyl-elastase 2 employed as tracer in the radioimmunoassay with alpha 2-macroglobulin, resulting in apparent immunoreactivity. These results demonstrate that all of the detectable immunoreactive pancreatic elastase 2 in normal human plasma is proelastase 2 bound to alpha 1-protease inhibitor.