[Stoichiometric protein-lipid interactions in liver microsomal membranes measured by the induction-resonance energy transfer method].

The stoichiometry of proteins and lipids in the microsomal membranes of the liver were studied by the induction-resonance energy transfer method. The energy was transferred between the fluorescent tryptophane residues of membrane proteins and fluorescent probes (pyrene and 4-dimethylaminochalcone) located in the microsomal lipid bilayer. It was assumed that the rate of protein fluorescence is correlated with protein mass. All microsomal proteins were arbitrarily divided into two groups, i.e. proteins located at a distance of more ("peripheral" proteins) and less than 30 A from the lipid bilayer surface. The former proteins made up to 14-24% of total microsomal protein, while microsomal ghosts--less than 10%. In the microsomes the bulk of other proteins is located at an average distance of about 19-26 A from the lipid bilayer surface, while the grosts--at about 4-9 A. Treatment of the ghosts with pronase results in approximation of the protein mass locus with the lipid by about 5 A. In this way the generation of ghosts and their treatment with pronase cause a loss of proteins predominantly from the peripheral parts of the microsomal membrane.