Phosphorescence Reveals a Continued Slow Annealing of the Protein Core following Reactivation of Escherichia coli Alkaline Phosphatase

When Escherichia coli alkaline phosphatase (AP) is refolded in vitro after extensive denaturation in 6.2 M guanidine hydrochloride, the enzymatic activity reaches its asymptotic value in 1 h at 24 degrees C. In contrast, the structural rigidity of the hydrophobic core of the protein, monitored by th...

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Veröffentlicht in:	Biochemistry (Easton) 1995, Vol.34 (4), p.1133-1136
Hauptverfasser:	Subramaniam, Vinod, Bergenhem, Nils C. H, Gafni, Ari, Steel, Duncan G
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline Phosphatase - chemistry Escherichia coli Escherichia coli - enzymology Guanidine Guanidines - chemistry Kinetics Luminescent Measurements Protein Denaturation Protein Folding Protein Structure, Tertiary
Online-Zugang:	Volltext
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