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

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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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fluorophosphate
Phosphatidylcholine-Sterol O-Acyltransferase
Peptides
aspartyl-proline
Pepsin A
Protein Sequence Analysis
High performance liquid chromatography
Enzymes
High Pressure Liquid Chromatography
Plasmas
Amino Acids

Cite this

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title = "The catalytic center of lecithin: Cholesterol acyltransferase: Isolation and sequence of diisopropyl fluorophosphate-labeled peptides",
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.",
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The catalytic center of lecithin : Cholesterol acyltransferase: Isolation and sequence of diisopropyl fluorophosphate-labeled peptides. / Park, Yong B.; Yüksel, K. Ümit; Gracy, Robert W.; Lacko, Andras G.

In: Biochemical and Biophysical Research Communications, Vol. 143, No. 1, 27.02.1987, p. 360-363.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The catalytic center of lecithin

T2 - Cholesterol acyltransferase: Isolation and sequence of diisopropyl fluorophosphate-labeled peptides

AU - Park, Yong B.

AU - Yüksel, K. Ümit

AU - Gracy, Robert W.

AU - Lacko, Andras G.

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AB - 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.

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