THE TOPOGRAPHY OF ACETYLCHOLINESTERASE IN DIMYRISTOYLPHOSPHATIDYLCHOLINE LIPOSOMES

Authors
  1. Barber, R.F.
  2. Stuhne-Sekalec, L.
  3. Shek, P.N.
  4. Stanacev, N.Z.
Corporate Authors
Defence and Civil Inst of Environmental Medicine, Downsview ONT (CAN);Toronto Univ, Toronto ONT (CAN) Dept of Clinical Biochemistry
Abstract
Unilamellar liposomes prepared from sn-3-(dimyristoyl)phosphatidylcholine (DMPC) in the presence and absence of acetylcholinesterase were examined by ESR for lipid/protein interactions. Using 5-, 12-, and 16-doxyl stearic acid probes incorporated into the phospholipid bilayers, no measurable differences in the gel to liquid-crystalline phase transition temperature of DMPC (as determined by ESR spectroscopy) were observed when the enzyme was present. These results have established that no significant incorporation of acetylcholinesterase into the hydrophobic region of the phospholipid bilayer is detectable at the protein: lipid ratios used in these experiments.
Report Number
DCIEM-89-P-01 — Research Paper; Reprint
Date of publication
01 Jan 1989
Number of Pages
9
Reprinted from
J Microencapsulation, vol 6, no 3, 1989, p 301-309
DSTKIM No
89-03138
CANDIS No
61039
Format(s):
Hardcopy;Originator's fiche received by DSIS

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