|
KMID : 0578319940040040529
|
|
Molecules and Cells
1994 Volume.4 No. 4 p.529 ~ p.533
|
|
|
Production of Specific Antibodies against Human Cholesteryl Ester Transfer Protein Using C-Terminal Active Peptide Obtained by Fusional Expression of Cholesteryl Ester Transfor Protein cDNA
|
|
Jeong, Nam Wook
Yoon, Woo Hyun/Choi, Myung-Sook/Huh, Tae-Lin/Yoon, Chang Soon/Kwak, Ju-Won/Bok, Song-Hee
|
|
|
Abstract
|
|
|
|
Partial (94 by from 3´ end) cDNA for cholesteryl ester transfer protein (CETP), obtained from a full-length cDNA clone isolated from a human heart Xgt11 cDNA library, was subcloned into a plasmid, pGEX, for the production of glutathione-S-transferase (GST)/CETP fusion proteins in Escherichia coh. The fusion protein, containing the carboxylic terminus of the CETP (31 amino acids) responsible for substrate binding of CETP, was produced as a soluble form in a large quantity. The soluble GST/CETP protein was further purified by glutathione-Sepharose4B affinity chromatography and used as an antigen for the production of the rabbit polyc-Ional antibody. The resulting antibody showed good titers, not only against the GST/CETP fusion protein, but also against chemically synthesized CETP-specific peptides (16 amino acids) having the internal sequences of the C-terminal region of CETP, as determined by ELISA. The antiserum would be useful for overcoming the difficulty of CETP purification and as an immunological tool for CETP assay in future studies.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|