Unfolding and Refolding of Coprinus cinereus Peroxidase at High pH, in Urea, and at High Temperature. Effect of Organic and Ionic Additives on These Processes

The unfolding and refolding rates of the heme- and Ca2+-containing Coprinus cinereus peroxidase (CIP) have been measured at pH 12.1, in 4 M urea, and at 61.2 °C. The change in peroxidase activity paralleled the change in the Soret band absorbance of the heme group. The unfolding rate constant (k u),...

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Veröffentlicht in:	Biochemistry (Easton) 1996-06, Vol.35 (23), p.7573-7579
Hauptverfasser:	Tams, Jeppe W, Welinder, Karen G
Format:	Artikel
Sprache:	eng
Schlagworte:	Coprinus - enzymology Coprinus cinereus Edetic Acid - pharmacology Enzyme Stability Hot Temperature Hydrogen-Ion Concentration Kinetics Peroxidases - chemistry Peroxidases - metabolism Protein Denaturation Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Thermodynamics Urea
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