[Study of the spatial structure of the protein component of the carcino-embryonic antigen by circular dichroism, Raman spectroscopy and UV-spectroscopy].
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.
Odinokov
S E
SE
Nabiullin
A A
AA
Glazunov
V P
VP
Kurika
A V
AV
Pavlenko
A F
AF
D002272:Carcinoembryonic Antigen; D002942:Circular Dichroism; D000939:Epitopes; D006023:Glycoproteins; D006801:Humans; D009363:Neoplasm Proteins; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman
D002272:Carcinoembryonic Antigen; D000939:Epitopes; D006023:Glycoproteins; D009363:Neoplasm Proteins
Issledovanie prostranstvennoĭ struktury belkovogo komponenta rakovo-émbrional'nogo antigena metodami KR, KD i UF-spektroskopii.