IDENTIFICATION OF A PUTATIVE MEMBRANE-INTERACTING DOMAIN OF CTP-PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE FROM RAT-LIVER

被引：31

作者：

WIEDER, T

GEILEN, CC

WIEPRECHT, M

BECKER, A

ORFANOS, CE

机构：

[1] FREE UNIV BERLIN,MED CTR STEGLITZ,DEPT DERMATOL,D-12200 BERLIN,GERMANY

[2] FREE UNIV BERLIN,DEPT MOLEC BIOL & BIOCHEM,D-14195 BERLIN,GERMANY

[3] SCHERING AG,INST MOLEC & CELLULAR BIOL,W-1000 BERLIN,GERMANY

来源：

FEBS LETTERS | 1994年 / 345卷 / 2-3期

关键词：

CTP; PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE; MEMBRANE BINDING; PEPTIDE-SPECIFIC ANTIBODY;

D O I：

10.1016/0014-5793(94)00433-1

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：

A putative membrane-interacting domain of CTP:phosphocholine cytidylyltransferase (CT) was identified using two peptide-specific antibodies. One antibody (SA2) was raised against the N-terminus of CT (amino acid residues 1-17) and the other antibody (SA209) against an alpha-helical domain of the enzyme (amino acid residues 247-257). Both antibodies quantitatively immunoprecipitated CT from rat liver cytosol and showed specificity towards CT when octylglucoside extracts of rat liver cytosol were assessed by Western blot analysis. However, further experiments revealed that the antibodies had different characteristics. Whereas the antibody directed against the N-terminus of CT (SA2) did not influence CT/membrane interaction, the new antibody (SA209) against the alpha-helical domain of the enzyme interfered with this interaction. Our results provide experimental evidence that the alpha-helical domain (amino acid residues 228-287) of CT may serve as a membrane-interacting domain.

引用

页码：207 / 210

页数：4

共 27 条

[1] CELL-SURFACE GLYCOPROTEINS OF HEPATOCYTES AND HEPATOMA-CELLS IDENTIFIED BY MONOCLONAL-ANTIBODIES [J].