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Thermodynamics of Denaturation of Horseradish Peroxidase with Sodium N-dodecyl Sulphate and N-dodecyl Trimethylammonium Bromide by A.A. Moosavi-Movahedi; K. Nazari; A.A. Saboury is a Materials Science article available to read on EtoBox.

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The interaction of sodium n-dodecyl sulphate (SDS) and n-dodecyl trimethylammonium bromide (DTAB) with horseradish peroxidase (HRP) at various pH values (3.2, 6.4 and 10.0) and temperatures (20-30'C) has been studied over a range of ligand concentrations using the difference spectroscopy technique. Data from ligand denaturation and thermal profiles of HRP were used to estimate the thermodynamic parameters AG, AH m, ACp, Tm, Ts, AG(H20) and [ligand]l~2 for the denaturation process. At pH 6.4 the enzyme was found to be more stable than at acidic and basic pH. In addition, data related to the unfolding of HRP in the presence of surfactants provided good agreement when analysed on the basis of linear extrapolation method and Tanford's model. ,

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Author

A.A. Moosavi-Movahedi; K. Nazari; A.A. Saboury

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0927-7765)

Published

1997

Language

EN

Field

Materials Science (Physical Sciences)