Trophoblast-specific beta 1-glycoprotein: its spatial structure and localization of antigenic determinants.
Effects of temperature and pH on the spatial structures of trophoblast-specific beta 1-glycoprotein (TSG) and its various derivatives and fragments have been studied by circular dichroic spectroscopy. The spatial organization of the protein portion of TSG derivatives, as revealed by the spectroscopic evidence, has been discussed with respect to the antigenic activity of the species studied. We concluded that the TSG protein portion consists mainly of a beta-structural type. The antigenic determinants were shown to be topographic, and are preferentially localized in the protein portion; only about 15% of the TSG antigenic activity failed to bear a direct relation to the spatial structure. The antigenic determinants seemed to include a tryptophan residue.
Pavlenko
A F
AF
Pacific Institute of Bioorganic Chemistry, Academy of Sciences, Vladivostok, USSR.
Moroz
S V
SV
Glazunov
V P
VP
Vakorina
T I
TI
Belogortseva
N I
NI
Odinokov
S E
SE
Ovodov YuS
D002942:Circular Dichroism; D000939:Epitopes / Q000032:analysis*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008745:Methylation; D015394:Molecular Structure; D011033:Podophyllin / Q000031:analogs & derivatives*; D011034:Podophyllotoxin / Q000031:analogs & derivatives; D011487:Protein Conformation; D013696:Temperature; D013774:Tetranitromethane; D014443:Tyrosine / Q000032:analysis
D000939:Epitopes; D014443:Tyrosine; C003170:mitopodozide; D011033:Podophyllin; D013774:Tetranitromethane; D011034:Podophyllotoxin