Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Wild-type recombinant horseradish peroxidase purified and refolded from Escherichia coli inclusion bodies has been studied in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (Aerosol OT)-reversed micelles in octane. In contrast with native horseradish peroxidase the wild-type recombinant...

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Veröffentlicht in:	Biochemical journal 1997-12, Vol.328 ( Pt 2) (2), p.643-647
Hauptverfasser:	Gazaryan, I G, Klyachko, N L, Dulkis, Y K, Ouporov, I V, Levashov, A V
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Catalysis Dimerization Dioctyl Sulfosuccinic Acid Horseradish Peroxidase - chemistry Horseradish Peroxidase - genetics Horseradish Peroxidase - metabolism Micelles Models, Molecular Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Structure-Activity Relationship Surface-Active Agents
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