PROTEIN-PROTEIN INTERACTIONS IN REVERSE MICELLES - TRYPSIN SHOWS SUPERACTIVITY TOWARDS A PROTEIN SUBSTRATE ALPHA-CHYMOTRYPSINOGEN-A IN REVERSE MICELLES OF SODIUM BIS(2-ETHYLHEXYL)SULFOSUCCINATE (AOT) IN ISOOCTANE

Protein-protein interactions in reverse micelles of sodium bis(2-ethyl hexyl)sulfosuccinate (AOT), in isooctane containing varying amounts of Tris buffer are studied by using activation of alpha-chymotrypsinogen A by trypsin (EC 3.4.21.4) to alpha-chymotrypsin (EC 3.4.21.1) as a m odel reaction. It has been found that protein-protein interactions are strongly dependent on the water content of the medium. At an optimum water content the activation reaction in reverse micelles is faster th an reaction in water by a factor of 21.3. At lower water content both reaction rates and the conversion of alpha-chymotrypsinogen A into alp ha-chymotrypsin decrease with decrease in water content of the reactio n medium.