A Histidine-rich Metal Binding Domain at the N Terminus of Cu,Zn-Superoxide Dismutases from Pathogenic Bacteria

A group of Cu,Zn-superoxide dismutases from pathogenic bacteria is characterized by histidine-rich N-terminal extensions that are in a highly exposed and mobile conformation. This feature allows these proteins to be readily purified in a single step by immobilized metal affinity chromatography. The...

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Veröffentlicht in:	The Journal of biological chemistry 2001-08, Vol.276 (32), p.30315-30325
Hauptverfasser:	Battistoni, Andrea, Pacello, Francesca, Mazzetti, Anna Paola, Capo, Concetta, Kroll, J. Simon, Langford, Paul R., Sansone, Assunta, Donnarumma, Giovanna, Valenti, Piera, Rotilio, Giuseppe
Format:	Artikel
Sprache:	eng
Online-Zugang:	Volltext
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