Abstract

Rat apolipoproteins C-II, C-III-0 and C-III-3 give similar surface pressure (π)— molecular area isotherms when spread at the air/water interface. When allowed to adsorb to the clean air/water interface, the intrinsic surface activity of apolipoprotein C-II is somewhat higher than that of apolipoprotein C-III. All three apolipoprotein C molecules can penetrate an egg phosphatidylcholine monolayer spread at the air/water interface causing an increase (Δπ) in surface pressure. Increasing the initial surface pressure (π i) of the lipid monolayer decreases Δπ, and Δπ = 0 when π i ⩽ 32 ± 2 mN· m −1 for all three apolipoprotein C proteins. This implies that apolipoproteins C-II, C-III-0 and C-III-3 would adsorb and desorb similarly from the surfaces of lipoprotein particles during metabolism.

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