Thermally induced conformational changes in horseradish peroxidase

Detailed differential scanning calorimetry (DSC), steady‐state tryptophan fluorescence and far‐UV and visible CD studies, together with enzymatic assays, were carried out to monitor the thermal denaturation of horseradish peroxidase isoenzyme c (HRPc) at pH 3.0. The spectral parameters were compleme...

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Veröffentlicht in:	European journal of biochemistry 2001-01, Vol.268 (1), p.120-126
Hauptverfasser:	Pina, David G., Shnyrova, Anna V., Gavilanes, Francisco, Rodríguez, Anabel, Leal, Fernando, Roig, Manuel G., Sakharov, Ivan Y., Zhadan, Galina G., Villar, Enrique, Shnyrov, Valery L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Calorimetry Circular Dichroism differential scanning calorimetry horeseradish peroxidase Horseradish Peroxidase - chemistry Hydrogen-Ion Concentration intrinsic fluorescence irreversible denaturation Protein Conformation Protein Denaturation Spectrometry, Fluorescence Temperature
Online-Zugang:	Volltext
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