Abstract
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.
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