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J. Biol. Chem., Vol. 265, Issue 36, 22123-22129, Dec, 1990
A Jonas, JH Wald, KL Toohill, ES Krul and KE Kezdy
We prepared a spherical reconstituted high density lipoprotein (rHDL)
particle in pure form and compared it with its homogeneous discoidal rHDL
precursors, in terms of the structure and stability of the apolipoprotein
A-I (apoA-I) component, the dynamics of the surface lipids, and the
relative reactivity with lecithin-cholesterol acyltransferase. The
apoA-I-structure was examined in the rHDL particles by circular dichroism
and fluorescence spectroscopic methods, and the binding of monoclonal
antibodies specific for apoA-I epitopes. The stability of apoA-I on the
rHDL particles was assessed by the effects of guanidine hydrochloride on
the wavelength of maximum intrinsic fluorescence of the apolipoprotein.
Lipid dynamics in the acyl chain region and the polarity of the lipid-water
interface were investigated by means of fluorescence probes. The
conformation of apoA- I in the spherical 93-A rHDL particles was found to
be very similar to that in the 96-A rHDL discs but distinct from the apoA-I
structure in the 78-A rHDL discs. The stability of apoA-I to denaturation
by guanidine hydrochloride was highest in the 93-A rHDL spheres. The
experiments on the lipids indicate somewhat more ordered and motionally
restricted acyl chains in the spheres, relative to the discs, but a similar
surface polarity. These results suggest that the folding and organization
of apoA-I on the three particles include protein domains consisting of
interacting alpha-helical segments in the carboxyl- terminal region and a
globular domain in the amino-terminal region of each apoA-I molecule. The
reactivity with lecithin-cholesterol acyltransferase was highest for the
96-A rHDL disc, and 16- and 34-fold lower for the 78-A rHDL disc and the
93-A rHDL sphere, respectively, possibly as a result of differences in
apoA-I structure and product inhibition in these particles.
Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins
Department of Biochemistry, College of Medicine, University of Illinois, Urbana 61801.
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