title: Phospholipase A2 activity in dehydrated systems: effect of the physical state of the substrate.
abstract: In the presence of excess water, enzymatic activity of phospholipase A2 (PLA2) depends on the physical state of the lipid substrate. In order to determine if this also holds true in dehydrated systems, the physical parameters of charge, hydration state, and head group spacing of liposome membranes and their effects on PLA2 lipid hydrolysis were studied. Liposomes of varying composition were freeze-dried in the presence of PLA2 and partially rehydrated at controlled relative humidities. Accumulation of free fatty acids in the liposomal membranes was used as a measure of PLA2 activity. We found that PLA2, which was not activated during lyophilization, was most active during partial rehydration of the liposomes. The hydration state, charge and headgroup spacing of the membrane were all important in determining PLA2 activity in the dehydrated system.
authors.affiliation: Section of Molecular and Cellular Biology, University of California, Davis 95616, USA.
authors.forename: A E
authors.initials: AE
authors.lastname: Oliver
authors.forename: E
authors.initials: E
authors.lastname: Fisk
authors.forename: L M
authors.initials: LM
authors.lastname: Crowe
authors.forename: P S
authors.initials: PS
authors.lastname: de Araujo
authors.forename: J H
authors.initials: JH
authors.lastname: Crowe
mesh_terms: D005230:Fatty Acids, Nonesterified; D008051:Lipid Bilayers / Q000737:chemistry*; D010741:Phospholipases A / Q000737:chemistry*; D054467:Phospholipases A2; D014867:Water
chemical_list: D005230:Fatty Acids, Nonesterified; D008051:Lipid Bilayers; D014867:Water; D010741:Phospholipases A; D054467:Phospholipases A2