Kinetic approach to the interaction of sodium n-dodecyl sulphate with heme enzymes

• Published in: International journal of biological macromolecules Vol. 24; no. 1; pp. 69 - 74
• Main Author: Gebicka, L
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 1999
• Subjects: Animals; Catalase; Catalase - chemistry; Cattle; Circular Dichroism; Dose-Response Relationship, Drug; Edetic Acid - metabolism; Heme - chemistry; Horseradish peroxidase; Horseradish Peroxidase - chemistry; Hydrogen-Ion Concentration; Kinetics; Liver - enzymology; Micelle; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; SDS; Sodium Dodecyl Sulfate - chemistry; Spectrophotometry; Stopped-flow; Time Factors; Horseradish peroxidase; Micelle; SDS; Catalase; Stopped-flow
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/S0141-8130(98)00071-3

The kinetics of interaction of sodium n-dodecyl sulphate (SDS) with catalase has been studied by absorbance and fluorescence changes. The results have been compared with circular dichroism spectra and activity measurements. The tertiary structure of catalase is modified by SDS in the monomeric and micellar form. The secondary structure of catalase is altered only in the presence of SDS micelles. On the other hand, neither spectroscopic properties nor activity of horseradish peroxidase change in the presence of SDS below micellar concentration. In the presence of SDS micelles, however, changes of secondary and tertiary structure of this protein are detected. The reason for relatively high stability of horseradish peroxidase in the presence of SDS is discussed.