TY - JOUR
T1 - Isolation, chemical characterization, and biophysical properties of three different abnormal lipoproteins
T2 - LP X1, LP X2, and LP X3
AU - Patsch, J. R.
AU - Aune, K. C.
AU - Gotto, A. M.
AU - Morrisett, J. D.
PY - 1977
Y1 - 1977
N2 - Three different but related abnormal lipoprotein species, LP X1, LP X2, and LP X3, have been isolated from cholestatic plasma by ethanol precipitation and zonal ultracentrifugation. All three populations are rich in phospholipids (64.9 to 67.5%) and cholesterol (23.0 to 26.8%) but poor in cholesteryl esters (0.4 to 1.9%), triglycerides (1.8 to 3.2%), and protein (3.2 to 6.7%) with differences in chemical composition which result in buoyant densities (1.038, 1.049, and 1.058, respectively) to allow their separation. LP X1, LP X2, and LP X3 exhibited apparent flotation rates of 17.3, 9.7, and 3.2 Svedbergs and Stokes radii of 339, 343, and 294 Å, respectively. As determined from circular dichroic measurements, the protein constituents of all three particles possessed a high degree of α helical structure (41 to 65%). Each LP X particle exhibited abnormally low fluidity as evaluated by electron paramagnetic resonance. All of the particles contained human serum albumin and the C proteins as major protein constituents, but only LP X2 and LP X3 contained apolipoprotein A I and apolipoprotein E.
AB - Three different but related abnormal lipoprotein species, LP X1, LP X2, and LP X3, have been isolated from cholestatic plasma by ethanol precipitation and zonal ultracentrifugation. All three populations are rich in phospholipids (64.9 to 67.5%) and cholesterol (23.0 to 26.8%) but poor in cholesteryl esters (0.4 to 1.9%), triglycerides (1.8 to 3.2%), and protein (3.2 to 6.7%) with differences in chemical composition which result in buoyant densities (1.038, 1.049, and 1.058, respectively) to allow their separation. LP X1, LP X2, and LP X3 exhibited apparent flotation rates of 17.3, 9.7, and 3.2 Svedbergs and Stokes radii of 339, 343, and 294 Å, respectively. As determined from circular dichroic measurements, the protein constituents of all three particles possessed a high degree of α helical structure (41 to 65%). Each LP X particle exhibited abnormally low fluidity as evaluated by electron paramagnetic resonance. All of the particles contained human serum albumin and the C proteins as major protein constituents, but only LP X2 and LP X3 contained apolipoprotein A I and apolipoprotein E.
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M3 - Article
C2 - 191454
AN - SCOPUS:0017332490
SN - 0021-9258
VL - 252
SP - 2113
EP - 2120
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 6
ER -