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KMID : 0578319910010020235
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Molecules and Cells
1991 Volume.1 No. 2 p.235 ~ p.239
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Purification of Pregnancy-specific Beta-1 Glycoprotein from Human Placenta and Prodction of Its Monoclonal Antibody
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Lee, Jae Ho
Chung, Jun Ho/Chung, Hong keun
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Abstract
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SPI, one of the pregnancy-specific proteins, was purified from the pregnancy sera using the methods of fractional salting-out, anion-exchange chromatography, Con-A affinity chromatography, Sephadex G-200 gel Filtration and HPLC. The purification was 200 fold and the yield was 5.5%. The purity was about 70% and the purified SPI was used as an immunogen for the production of monoclonal antibodies. Among the monoclonal antibodies produced, one was of IgG2. subtype and the other seven were of IgG, subtype. The specificity of the antibodies was assessed. Three antibodies reacted with three bands (68, 64 and 56 kDa) on the SPI SDS-polyacrylamide gel which were also recognized by polyclonal anti-SPI antibody.
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