Robert S, Domurado D, Thomas D, Chopineau J
Laboratoire de Technologie Enzymatique, URA CNRS 1442, Université de Technologie de Compiègne, France.
Biochem Biophys Res Commun. 1993 Oct 15;196(1):447-54. doi: 10.1006/bbrc.1993.2270.
A water soluble protein, RNAse A, was fatty-acylated using AOT reversed micelles in 2,2,4-trimethyl pentane as microreactors and myristoyl chloride as reagent. Artificial attachment of lipid molecules to this protein was performed for different hydration degrees by changing Wo = [water]/ [AOT], the parameter which controls the microreactor size. The chemically modified protein was monitored using reverse phase HPLC and characterized by HPLC, free amino groups titration, and electrophoresis. An RNase A/myristoyl chloride ratio of 1:4 (mol/mol) at Wo = 7 was found to give 60% of modified protein.