THE CATALYTIC CENTER OF LECITHIN-CHOLESTEROL ACYLTRANSFERASE-ISOLATION AND SEQUENCE OF DIISOPROPYL FLUOROPHOSPHATE-LABELED PEPTIDES

被引：9

作者：

PARK, YB ^{[1
]}

YUKSEL, KU ^{[1
]}

GRACY, RW ^{[1
]}

LACKO, AG ^{[1
]}

机构：

[1] N TEXAS STATE UNIV, TEXAS COLL OSTEOPATH MED, DEPT BIOCHEM, FT WORTH, TX 76107 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1987年 / 143卷 / 01期

关键词：

D O I：

10.1016/0006-291X(87)90673-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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-Lue-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.

引用

页码：360 / 363

页数：4

共 11 条

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