Keywords

Glycinin, A1A Acidic Peptide, Prokaryotic Expression, B Cell Epitope

Abstract

? In order to provide basic materials for the establishment of glycinin immunoassay methods and in-depth research on the sensitization mechanism, the cdna sequence of the glycinin a1a acidic polypeptide gene was artificially synthesized and constructed through polymerase chain reaction (PCR) and bamhi and kpni double enzyme digestion. The prokaryotic expression vector pet30a-a1a was obtained, and the recombinant plasmid was transformed into Escherichia coli (e.coli) bl21 and then induced with isopropylthio-¦Â-d-galactopyranoside (iptg). SDS-PAGE analysis showed that the a1a acidic polypeptide fusion protein can be secreted and expressed in the form of a soluble protein, and the expression level of the a1a acidic polypeptide fusion protein reached the highest level after 5 hours of induction. After purification by His affinity chromatography, a fusion a1a protein with a purity of 90% was obtained, with a molecular mass of approximately 38kd. Western blotting showed that the obtained a1a fusion protein could produce an immune reaction with the serum of piglets allergic to soybean meal, indicating that the obtained fusion protein had immune activity.

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Original research done by Liu Bin, Teng Da, Yang Yalin, Wang Jianhua

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