Dimerization of recombinant horseradish peroxidase in a reversed micellar systemстатья
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 7 октября 2013 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:1128
Последняя страница:1134
Аннотация:Recombinant horseradish peroxidase reactivated from E. coil inclusion bodies was studied in a reversed micellar system of AOT in octane. The ability of the recombinant enzyme, in contrast to native horseradish peroxidase, to form a dimeric structure was found. The existence of the dimer was proved by results of sedimentation analysis. Dimer/monomer ratio in the enzyme-containing micelles and dimer catalytic activity were found to depend on the substrate used (pyrogallol, guaiacol, o-dianisidine, o-phenylenediamine). Computer modelling was used to describe possible structures of the dimeric recombinant horseradish peroxidase.