Abstract
Hydrolysis of chloramphenicol palmitate (CPP) in insoluble monolayer in the presence of lipase in aqueous subphase has been studied by simultaneous determination of molecular area A of CPP and surface radioactivity R as a function of time t under a constant surface pressure. Separate use of CP- 14C-P and CPP- 14C, i.e., CPP samples isotopically labeled at hydrophilic and hydrophobic positions, respectively, made it possible to analyze the A ∼ R ∼ t relationship, which reflects the enzymatic reaction to be governed solely by the adsorbed amount of lipase and the fraction of CPP in the α conformation.
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