Isolation, Purification and Characterization of Human serum Apolipoprotein AI
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    Abstract:

    Apolipoprotein AI(apo AI) was separated and purified from human serum by precipitation with dextran sulphate 500(DS 500), density gradient zonal ultracentrifugation,delipidation and Sephadex G150 gel permeation chromatography.Identifying by SDS-posyacrylamide gel electrophoresis (SDS-PAGE)and analytical islelectric focusing (IEF),the purified apo AI shows only one band on SDS-PAGE, and the molecular weight is 28 180. With DS 500 sedimentation,this method saves time for ultracentrifugation,which is much valuable for large-amount purification of apo AI.

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LIU Shang-Xi, CHEN Yuan, ZHOU Mei. Isolation, Purification and Characterization of Human serum Apolipoprotein AI[J]. Editorial Office of Chinese Journal of Arteriosclerosis,1996,4(2):136-139.

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History
  • Received:February 01,1996
  • Revised:May 25,1996
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