Abstract
SUMMARYThe surface characteristics of plasma low‐density lipoprotein (LDL) in various buffers were investigated by determining the binding of an anionic dye, methyl orange, during equilibrium dialysis at 10°. As the buffer pH increased from 4.5 to 8.6, the binding capacity of native LDL diminished. Additional experiments were carried out at pH 6.5, the normal value for egg yolk and plasma. A plot of dye concentration vs. dye binding by native LDL produced a curve with a shape similar to that for ‐β lipoprotein from blood. Native LDL, with only about 15% protein, bound as much dye as a pure protein, β‐lactoglobulin. The LDL from pasteurized yolk (63 and 64.8°C) bound as much dye as LDL from native yolk. Sodium chloride and sucrose did not restrict the dye adsorption to native LDL. When yolk plasma was treated with bromelain, the dye‐binding capacity of isolated LDL was somewhat reduced.
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