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

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 m...

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Published inInternational journal of biological macromolecules Vol. 24; no. 1; pp. 69 - 74
Main Author Gebicka, L
Format Journal Article
LanguageEnglish
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
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Abstract 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.
AbstractList 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.
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.
Author Gębicka, Lidia
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Cites_doi 10.1007/s007750050123
10.1016/0005-2795(77)90047-2
10.1016/S0021-9258(17)38904-4
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Keywords Horseradish peroxidase
Micelle
SDS
Catalase
Stopped-flow
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Snippet The kinetics of interaction of sodium n-dodecyl sulphate (SDS) with catalase has been studied by absorbance and fluorescence changes. The results have been...
The kinetics of interaction of sodium n-dodecyl sulphate (SDS) with catalase has been studied by absorbance and fluorescence changes. The results have been...
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StartPage 69
SubjectTerms 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
Title Kinetic approach to the interaction of sodium n-dodecyl sulphate with heme enzymes
URI https://dx.doi.org/10.1016/S0141-8130(98)00071-3
https://www.ncbi.nlm.nih.gov/pubmed/10077275
https://search.proquest.com/docview/69625156
Volume 24
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