Synthesis and use of a lysolecithin analog for the purification of UDP-glucuronosyltransferase

Andrew Dannenberg, Timothy Wong, David Zakim, Hansjorg Eibl

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Because of their high cost, lysolecithins are generally not considered useful detergents for the purification of membrane-bound enzymes. Therefore, we have synthesized a structural analog of lysolecithin with similar physical properties for which synthesis is straightforward. This analog is 1-palmitoylpropanediol-3-phosphocholine. To compare the efficacy of the two detergents for the purification of a membrane-bound enzyme, we have purified UDP-glucuronosyltransferase from pig liver microsomes using lysophosphatidylcholine or the synthetic analog. The catalytic properties of UDP-glucuronosyltransferase purified with 1-palmitoylpropanediol-3-phosphocholine or lysolecthin were identical. Sodium dodecyl sulfate-gel electrophoresis indicated that the purity of the UDP-glucuronosyltransferase preparation was the same whether lysophosphatidylcholine or its synthetic analog was used. The advantage of using 1-palmitoylpropanediol-3-phosphocholine in preference to lysophosphatidylcholine is that the former can be synthesized for about 1% the cost of the latter. In addition, the method for synthesis of 1-palmitoylpropanediol-3-phosphocholine is general in that the structural features of the polymethylene chain can be varied, allowing for the inexpensive synthesis of a series of detergents.

Original languageEnglish (US)
Pages (from-to)183-186
Number of pages4
JournalAnalytical Biochemistry
Volume191
Issue number1
DOIs
StatePublished - Nov 15 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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