[Extraction of horseradish peroxidase and its conjugates formed by surface-active agent micelles].
The author studied peculiarities of the extraction of horseradish peroxidase (HRP) and its conjugates with 3 and 7 molecules of progesterone (PROG) from the aqueous solution into heptane and chloroform containing reversed micelles of surfactants. Micelles of cetyltrimethylammonium bromide, Aerosol OT, and Triton X-45 protect the enzyme from denaturation in the biphasic system. The enzyme is readily extracted from the aqueous phase in the organic medium containing reversed micelles of surfactants at low values of pH. The addition of PEG-6000 (5%) to the aqueous phase enhances the enzyme solubilization at pH 8.6-9.0. The enzyme solubilization significantly increases, when surfactants with unlike charges are used. Inorganic salts decrease the specific solubilization of the enzyme. The HRP modification with progesterone has a weak effect on the enzyme solubilization with reversed micelles.
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D006735:Horseradish Peroxidase / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007150:Immunohistochemistry; D008823:Micelles; D011374:Progesterone / Q000737:chemistry; D012997:Solvents; D013501:Surface-Active Agents / Q000737:chemistry*
D008823:Micelles; D012997:Solvents; D013501:Surface-Active Agents; D011374:Progesterone; D006735:Horseradish Peroxidase
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