Sphingomyelinase acts by an area-activated mechanism on the liquid-expanded phase of sphingomyelin monolayers

LUISINA DE TULLIO; BRUNO MAGGIO; MARÍA LAURA FANANI

JLR PAPERS IN PRESS

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Año: 2008 vol. 49 p. 2347 - 2347

span style="FONT-FAMILY: Arial; mso-ansi-language: EN-US" lang="en"> We described the localization of Alexa-488-labeled Sphingomyelinase (SMase) in sphingomyelin (SM)/ceramide (Cer) lipid monolayers containing segregated liquid-condensed (LC) Cer-enriched domains surrounded by a continuous liquid-expanded (LE) SM-enriched phase. Langmuir-Schaefer films were made in order to visualize the labelled enzyme. Independently of initial conditions Alexa-SMase is preferably localized in the SM-enriched LE phase and it is not enriched at the domain boundaries.