The catalytic center of lecithin: Cholesterol acyltransferase: Isolation and sequence of diisopropyl fluorophosphate-labeled peptides

Yong B. Park, K. Ümit Yüksel, Robert W. Gracy, Andras G. Lacko

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Lecithin: cholesterol acyltransferase (LCAT) was purified from hog plasma and subsequently reacted with [3H]-Diisopropyl fluorophosphate (DFP). The labeled enzyme was digested with pepsin and the peptides separated by high performance liquid chromatography (HPLC). Two radioactive peptides were isolated, subjected to automated amino acid sequencing and yielded the following data: A) Ile-Ser-Leu-Gly-Ala-Pro-Trp-Gly-Gly-Ser, and B) Tyr-Ile-Phe-Asp-x-Gly-Phe-Pro-Tyr-x-Asp-Pro-Val. Both of these sequences represent very highly conserved regions of the enzyme when compared to the sequence of human LCAT. Peptide (A) is considered to represent the catalytic center of LCAT based on comparisons with data reported in the literature.

Original languageEnglish
Pages (from-to)360-363
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume143
Issue number1
DOIs
StatePublished - 27 Feb 1987

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