Sk. Patra et al., DETERGENT SOLUBILIZATION OF PHOSPHOLIPID-BILAYERS IN THE GEL STATE - THE ROLE OF POLAR AND HYDROPHOBIC FORCES, Biochimica et biophysica acta. Biomembranes, 1373(1), 1998, pp. 112-118
Testing the solubilisation of phosphatidylcholine (PC) bilayers by Tri
ton X-100 reveals that in the gel state, but not in the fluid state, t
he amount of detergent required to solubilise the phospholipid is high
ly dependent on the chain length. Saturated C16 and C18 PC are virtual
ly insoluble at 4 degrees C. However, addition of water-soluble reagen
ts that perturb hydrogen bonding, e.g, urea, or of small proportions o
f non-bilayer lipids, make the bilayers amenable to detergent solubili
sation, even at low temperatures. These results are relevant in the ex
planation of the origin of detergent-resistant membrane fragments as f
ound, e.g. in caveolae or 'rafts'. (C) 1998 Elsevier Science B.V. All
rights reserved.