Conformational changes in intact and papain-modified alpha sub(1)-proteinase inhibitor induced by guanidinium chloride
Equilibrium unfolding--refolding processes of active and proteolytically modified alpha sub(1)-proteinase inhibitor induced by guanidinium chloride were studied. Spectroscopic methods of ultraviolet absorption, fluorescence emission and circular dichroism were used. The unfolding irreversibility obs...
Gespeichert in:
| Veröffentlicht in: | European journal of biochemistry 1990-01, Vol.191 (3), p.653-658 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| Zusammenfassung: | Equilibrium unfolding--refolding processes of active and proteolytically modified alpha sub(1)-proteinase inhibitor induced by guanidinium chloride were studied. Spectroscopic methods of ultraviolet absorption, fluorescence emission and circular dichroism were used. The unfolding irreversibility observed was attributed to the C-terminal fragment Ser359-Lys394 associated with the main chain of the cleaved inhibitor. |
|---|---|
| ISSN: | 0014-2956 |