| Autor: |
BOUSQUET, Jean-Alain, DURANTON, Jérôme, MÉLY, Yves, BIETH, Joseph G. |
| Zdroj: |
Biochemical Journal; February 2003, Vol. 370 Issue: 1 p345-349, 5p |
| Abstrakt: |
The CD spectrum of porcine pancreatic elastase in complex with α1-proteinase inhibitor (α1-PI) was calculated by subtracting the CD spectrum of the proteolytically cleaved inhibitor from that of the elastase—α1-PI complex. Elastase undergoes a moderate secondary structure change: its β-structure is partially disordered while its α-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 α1-PI observed by previous investigators. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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