Hydorphilic-hydrophobic properties and solubilization state of proteins in reverse micelles

摘要

Solubilization state of proteins, e.g. cytochrome c, lysozyme and ribonuclease A, in AOT reverse micelles was investigated. Extraction behavoir of protein was depended on protein species. Cytochrome c could be well solubilized into reverse micellar phase not only by two phase mixing but also by dropwise injection method. It obviously shoed apparent molecular conformational change in reverse micellar phase than other tested proteins. To elucidate the possibility which means proteins could be located in an amphiphles' layer of reverse micellar interface, an analysis of amino acid sequences of proteins was carried out. Cytochorome c has a higher possibility to exist at Amphiphilic layer of reverse micelles rather than other tested proteins.