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Recombinant cytochrome b5 was extracted to a reversed micelle phase of a cationic surfactant (hexadecyltrimethylammonium bromide, CTAB) in cyclohexane/decanol and back-extracted to a fresh aqueous phase. Depending on the experimental conditions, i.e., temperature, pH, and ionic strength, the extraction is controlled by either hydrophobic (pH close to the pI(More)
Recombinant cytochrome b5 was extracted into the reversed micelle phase of an anionic surfactant (AOT) in octane and back-extracted to a final aqueous phase. The extraction of the protein was controlled by an electrostatic mechanism, since it was dependent on the global charge of the protein. This was directly demonstrated by experiments with native and(More)
The mechanism of extraction of rat cytochrome b(5) from water into a sodium dioctylsulfosuccinate (AOT) micellar organic phase was studied using protein engineering of surface charged residues. The extraction behavior of native cytochrome b(5) and modified proteins with substitutions of the type glutamic acid --> lysine at positions 44 (E44K), 56 (E56K),(More)
The partitioning of cytochrome b5 in aqueous two-phase systems of polyethylene glycol (PEG) and potassium phosphate salts was investigated. Cytochrome b5 partitioning is enhanced with decreasing polymer molecular mass and with increasing tieline length and pH. The effect of cytochrome b5 mutation, by substitution of the glutamic acid at positions 56 and 92(More)
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