caa a22 4500 605536791 CHVBK 20210128100854.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s10517-015-3102-7 doi (NATIONALLICENCE)springer-10.1007/s10517-015-3102-7 Recombinant N-Domain of Pregnancy-Specific Glycoprotein from E. coli Cells: Analysis of the Spectrum of Polyclonal Antibodies [Elektronische Daten] [P. Prokopenko, A. Shkoporov, O. Petrenko, B. Efimov, V. Negrebetskii, A. Terent'ev] We studied antibody spectrum in antisera to IgG-like recombinant N-domain of pregnancyspecific glycoprotein-1 (rPSG-N) from E. coli cells. In three experimental series, the fraction of IgG antibodies from anti-rPSG-N sera was immobilized on 3 immunoadsorbents: by polymerization with glutaraldehyde, on glutaraldehyde activated biogel P-300, and on commercial CNBr-activated 4B sepharose. Retroplacental serum was incubated with immobilized antibodies to rPSG1-N, protein was eluted and tested in the precipitation test in standard test systems with PSG1, IgG, and human serum albumin. Three proteins were eluted from all 3 immunoadsorbents: PSG1, IgG, and human serum albumin, which demonstrated the spectrum of antibodies to 3 proteins present also in natural serum PSG1 complex. The proportions of PSG1 and IgG obtained in these experiments were similar to those in natural serum PSG1 complex, while the level of human serum albumin was significantly higher in natural PSG1 complex. Thus, we failed to obtain PSG1 monoprotein free from IgG and human serum albumin. Antigenic mosaicism of the polypeptide chain of IgG-like rPSG1-N relative to the antigenic polyvalence of the complex of three proteins present in bioactive preparation of natural serum PSG1 was discussed. Springer Science+Business Media New York, 2015 pregnancy - specific glycoprotein - 1 ( PSG1 ) nationallicence IgG - like N - domain nationallicence recombinant analog from E. coli cells nationallicence antibody spectrum nationallicence antigenic mosaicism of polypeptide chain nationallicence Prokopenko P. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Shkoporov A. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Petrenko O. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Efimov B. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Negrebetskii V. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Terent'ev A. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut Bulletin of Experimental Biology and Medicine Springer US; http://www.springer-ny.com 160/1(2015-11-01), 76-80 0007-4888 160:1<76 2015 160 10517 https://doi.org/10.1007/s10517-015-3102-7 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s10517-015-3102-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Prokopenko P. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 700 1- Shkoporov A. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 700 1- Petrenko O. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 700 1- Efimov B. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 700 1- Negrebetskii V. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 700 1- Terent'ev A. N. I. Pirogov Russian National Research Medical University, Moscow, Russia aut NATIONALLICENCE 773 0- Bulletin of Experimental Biology and Medicine Springer US; http://www.springer-ny.com 160/1(2015-11-01), 76-80 0007-4888 160:1<76 2015 160 10517