Separation of the apoprotein components of human very low density lipoproteins by ion-paired,reversed-phase high performance liquid chromatography |
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Authors: | W S Hancock C A Bishop A M Gotto D R K Harding S M Lamplugh J T Sparrow |
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Affiliation: | (1) Department of Chemistry, Biochemistry and Biophysics, Massey University, Palmerston North, New Zealand;(2) Department of Medicine, Baylor College of Medicine, Mail Station A601, 6565 Fannin, 77030 Houston, TX;(3) The Methodist Hospital, Mail Station A601, 6565 Fannin, 77030 Houston, TX;(4) Present address: American Heart Assn., USA |
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Abstract: | A number of crude apolipoprotein samples isolated from human very low density lipoproteins (VLDL) were analyzed by reversed
phase high performance liquid chromatography. The mobile phase consisted of a 1% solution of the polar ion-pairing reagent
triethylammonium phosphate. A slow, nonlinear gradient of acetonitrile (37–42%) was used to elute the apolipoproteins. The
order of elution was as follows: apolipoprotein Cx, apolipoprotein C-I, apolipoprotein C-III2, apolipoprotein C-III1, apolipoprotein C-III0 and apolipoprotein C-II. This order is consistent with the known polarity of the proteins, i.e., the most nonpolar, apolipoprotein
C-II, was the last to be eluted, whereas apolipoprotein C-I, with the lowest nonpolar surface area eluted first. The recovery
of the individual apolipoproteins was 80–95% and the individual peaks were characterized by amino acid analysis, UV absorption
spectra and chromatography of pure protein standards. |
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