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The CD spectrum of porcine pancreatic elastase in complex with alpha1-proteinase inhibitor (alpha1-PI) was calculated by subtracting the CD spectrum of the proteolytically cleaved inhibitor from that of the elastase-alpha1-PI complex. Elastase undergoes a moderate secondary structure change: its beta-structure is partially disordered while its alpha-helix content is poorly affected. In contrast, its tertiary structure undergoes a significant structural loosening upon complexation. These alterations have been compared with those following chemical and thermal unfolding of free elastase. Inhibitor-bound elastase and the denaturation intermediate of free elastase share secondary but not tertiary structural features. On the other hand, both free and complexed elastases undergo a single-step transition in tertiary structure upon thermal unfolding. These data are discussed in terms of the inhibition and structural modification of elastase induced by alpha1-PI observed by previous investigators.

Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation