Molecular and biochemical characterization of lecithin retinol acyltransferase

Alberto Ruiz, Anette Winston, Young Hee Lim, Bryant A. Gilbert, Robert R. Rando, Dean Bok

Research output: Contribution to journalArticlepeer-review

218 Citations (Scopus)


The enzyme responsible for conversion of all-transretinol into retinyl esters, the lecithin retinol acyltransferase (LRAT) has been characterized at the molecular level. The cDNA coding for this protein was cloned and its amino acid sequence deduced. LRAT is composed of a polypeptide of 230 amino acid residues with a calculated mass of 25.3 kDa. Tissue distribution analysis by Northern blot showed expression of a 5.0-kilobase transcript in the human retinal pigment epithelium as well as in other tissues that are known for their high LRAT activity and vitamin A processing. Affinity labeling experiments using specific compounds with high affinity for LRAT and monospecific polyclonal antibodies raised in rabbits against two peptide sequences for LRAT confirmed the molecular mass of LRAT as a 25-kDa protein. High performance liquid chromatography analysis of the reaction product formed by HEK-293 cells transfected with LRAT eDNA confirmed the ability of the transfected cells to convert [3H]all-trans-retinol into authentic [3H]all-trans-retinyl palmitate as chemically determined.

Original languageEnglish
Pages (from-to)3834-3841
Number of pages8
JournalJournal of Biological Chemistry
Issue number6
Publication statusPublished - 1999 Feb 5
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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