Oligomerization of N-terminal domain of carcinoembryonic antigen (CEA) expressed in Escherichia coli

Biochemical and Biophysical Research Communications
A Krop-WatorekH Nakazato

Abstract

The N-terminal domain of CEA, which is essential for cell adhesion activity and lacks cysteine residue, was expressed in Escherichia coli and purified from the solubilized inclusion bodies by DEAE-Sepharose and gel filtration chromatographies. The purified N-domain migrated in SDS-PAGE as a single 13-kDa band, whereas it migrated in non-SDS-PAGE as five distinct bands. The N-domain, analyzed by two-dimensional PAGE after cross-linking with DSS, migrated in multiple forms ranging from monomer to pentamer, showing unequivocally the presence of multimers in each band. The amount of monomer was distinctively the least among the oligomers in the non-SDS-PAGE. These results suggest that the N-domain of CEA molecule has a strong tendency to self-assemble that may convey the homophilic cell adhesion of CEA.

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Citations

May 24, 2006·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Hui-Ling HuShing-Yi Suen
May 9, 2006·International Journal of Biological Macromolecules·Noelia Sainz-PastorKerry Ann Chester
Oct 19, 2002·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Tony J C Harris, Chi-Hung Siu
Apr 5, 2011·Protein Expression and Purification·Hanna Czepczyńska-KrężelAnna Krop-Watorek

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