[Relation between the spatial structure and antigenic activity of trophoblast-specific beta1-glycoprotein].
Temperature- and pH-dependence of spatial structure of a native trophoblast-specific beta-glycoprotein (TSG), its desialated and deglycosylated derivatives, as well as of a fragment obtained by partial acid hydrolysis on the temperature and pH variations has been studied using CD and UV spectroscopy. Within the range 45-50 degrees C a conformational transition of the protein moiety of TSG, leading to partially reversible alterations in tertiary and secondary structures of this glycoprotein after cooling the solution to 20 degrees C has been found out. The results of spectral studies of the spatial structure of the TSG protein component have been compared with the data on antigen activity of native, temperature- and pH-denaturated, desialated, and deglycosilated TSG. It has been concluded that the protein moiety of TSG consists mainly of beta-structures; the greater part of antigen determinants of TSG is topographic and belongs to the protein component of TSG, and only 15% of antigen determinants are not connected with TSG's spatial structure.
D002942:Circular Dichroism; D000939:Epitopes / Q000032:analysis*; D006801:Humans; D011257:Pregnancy Proteins / Q000032:analysis*; D011268:Pregnancy-Specific beta 1-Glycoproteins / Q000032:analysis* / Q000276:immunology; D011487:Protein Conformation; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship
D000939:Epitopes; D011257:Pregnancy Proteins; D011268:Pregnancy-Specific beta 1-Glycoproteins
Issledovanie vzaimosviazi prostranstvennoĭ struktury i antigennoĭ aktivnosti trofoblastspetsificheskogo beta1-glikoproteina.