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-ethylhexyl)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 model 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 than reaction in water by a factor of 21.3. At lower water content both reaction rates and the conversion of alpha-chymotrypsinogen A into alpha-chymotrypsin decrease with decrease in water content of the reaction medium.
Fadnavis
N W
NW
Organic Division-II, Indian Institute of Chemical Technology, Hyderabad.
Chandraprakash
Y
Y
Deshpande
A
A
D002384:Catalysis; D002919:Chymotrypsinogen / Q000737:chemistry* / Q000378:metabolism; D004143:Dioctyl Sulfosuccinic Acid / Q000737:chemistry*; D007700:Kinetics; D008823:Micelles; D009795:Octanes / Q000737:chemistry; D013501:Surface-Active Agents; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism; D014867:Water / Q000737:chemistry
D008823:Micelles; D009795:Octanes; D013501:Surface-Active Agents; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; D002919:Chymotrypsinogen; D014357:Trypsin; C045798:2,2,4-trimethylpentane