[Spatial structure and antigenic activity of non-glycosylated forms of embryonal prealbumin-1 (EPA-1NG)].
The influence of temperature and pH on the spatial structure of EPA-1NG has been studied by means of circular dichroism and differential UV-spectroscopy, indicating the molecule to consist mainly of beta-structures. A conformational transition in the molecule was observed within the range of 40-50 degrees C. The further temperature elevation (up to 70 degrees C) was accompanied to the complete distortion of the parent conformation, which is reversed after cooling down to 20 degrees C. A correlation of the spectral data with the antigenic activity of genuine EPA-1NG and its carboxymethylated, heat-degraded and pH-denatured derivatives demonstrates that some antigenic determinants of EPA-1NG appear to be topographic.
Pavlenko
A F
AF
Bulgakov
A A
AA
Moroz
S V
SV
Ovodov
Iu S
IuS
D000941:Antigens / Q000737:chemistry*; D002942:Circular Dichroism; D000939:Epitopes / Q000737:chemistry; D005326:Fetal Proteins / Q000737:chemistry* / Q000276:immunology; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011228:Prealbumin; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D000941:Antigens; D000939:Epitopes; D005326:Fetal Proteins; D006023:Glycoproteins; D011228:Prealbumin; C031458:embryonic prealbumin