Study of the spatial structure of the protein component of the carcino-embryonic antigen by circular dichroism, Raman spectroscopy and UV-spectroscopy
Odinokov, S.E.; Nabiullin, A.A.; Glazunov, V.P.; Kurika, A.V.; Pavlenko, A.F.
Bioorganicheskaia Khimiia 11(10): 1315-1322
1985
ISSN/ISBN: 0132-3423 PMID: 2416321 Document Number: 245059
The spatial structure features of intact and deglycosylated carcino-embryonic antigen (CEA) have been studied by circular dichroism. Raman and UV-spectroscopy methods in order to elucidate a pattern and localization of CEA immunodominants. The temperature-induced changes in the spatial structure of the protein moiety were compared with data on the CEA immunochemical activity estimated by EIA procedure. A conformational transition was found within the 55-75 degrees range that produced irreversible alterations in the tertiary structure, while the secondary structure could be restored after lowering the temperature to 20 degrees C. Spectral studies of intact and deglycosylated CEA demonstrated that immunochemical activity, at least partly, was associated with the tertiary structure of the CEA protein portion.