PlumX Metrics
Embed PlumX Metrics

Purification and characterization of lipid transfer protein(s) from human lipoprotein-deficient plasma

Journal of Lipid Research, ISSN: 0022-2275, Vol: 23, Issue: 7, Page: 1058-1067
1982
  • 195
    Citations
  • 0
    Usage
  • 13
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    195
    • Citation Indexes
      195
      • CrossRef
        195
  • Captures
    13

Abstract Description

Lipid transfer activities from human plasma have been characterized to determine whether triglyceride and cholesteryl ester transfer proteins are identical. After sequential purification by phenyl-Sepharose, CM-cellulose, chromatofocusing, and gel filtration, both triglyceride and cholesteryl ester transfer activities were purified approximately 15,000-fold compared to lipoprotein-deficient plasma, with a 14% recovery of both transfer activities. The gel filtration fraction showed two bands, Mr 58,300 and 66,400, as determined by electrophoresis in sodium dodecyl sulfate. Two samples, each containing predominately one of the two bands, were obtained by selectively combining the eluates from the gel filtration column. The specific activities of triglyceride and cholesteryl ester transfer promoted by the larger protein were within 10% of those for the smaller protein. The relative rates of transfer for cholesteryl ester, triglyceride, retinyl ester, and cholesteryl ether for each fraction were the same. The transfer of triglyceride by either the large or small molecular weight component was almost completely inhibited by mercurial compounds, whereas cholesteryl ester transfer was relatively unaffected. We conclude that triglyceride and cholesteryl ester are transferred by the same plasma protein(s).

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know