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Journal of Lipid Research, Vol 33, 123-130, Copyright © 1992 by Lipid Research, Inc.
DL Sparks and MC Phillips
The electrophoretic mobilities of low density lipoprotein (LDL) and six
pure proteins in a 0.5% agarose gel have been compared to literature
electrophoretic mobility values determined by the Tiselius moving boundary
method. There is a strong correlation (r = 0.99) between the
electrophoretic mobilities determined by the two techniques. The
electrophoretic behavior of charged particles smaller than very low density
lipoproteins (VLDL) is not markedly perturbed by a 0.5% agarose matrix, and
variations in mobility primarily reflect differences in particle valence
and density of surface charge. Application of electrokinetic theory to
derive protein and lipoprotein net charges from the electrophoretic
mobilities in agarose yields a quantitative delineation of lipoprotein
electrophoretic migration patterns wherein the beta mobility region
comprises a surface potential range of -4.5 to -7.0 mV; the pre-beta region
a range of -7.0 to -10.5 mV; the alpha mobility region a range of -10.5 to
-12.5 mV and the serum albumin region a range of -12.5 to -14.0 mV. Because
protein conformation and charge are critical in metabolic regulation, the
agarose gel electrophoresis technique provides a valuable analytical tool
that should help to elucidate further details of the structure-function
relationships of serum lipoprotein particles.
ARTICLES
Quantitative measurement of lipoprotein surface charge by agarose gel electrophoresis
Department of Physiology and Biochemistry, Medical College of Pennsylvania, Philadelphia 19129.
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