Abstract
The exchange of unesterified cholesterol molecules between rat erythrocyte "ghosts" and human low-density lipoproteins was studied under a number of different experimental conditions. The process is pH-dependent, the rate being minimal at about pH 5. Cholesterol exchange does not vary greatly with temperature, the rate at 50[degree] being less than twice that at 2[degree]. Large variations in the ionic strength or Ca2+ concentration of the medium have little effect, but the exchange rate is greatly increased in the presence of a wide range of chemical compounds, e.g. urea, alcohols, acetone, dimethyl sulphoxide and tetra-alkyl-ammonium salts. Acetone and dimethyl sulphoxide have a much greater effect at 37[degree] than at 8-10[degree]. It is proposed that hydrophobic bonding is of great importance in maintaining the structure of "ghosts" and lipoproteins. The results are discussed in relation to current theories of membrane and lipoprotein structure.

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