Abstract

Aspergillus flavus is a ubiquitous filamentous fungus, which contaminates crops, also causes severe disease in animals. The well conserved representative of the ubiquitin-like family SUMO (small ubiquitin-like modifier) is associated with the superfamily of ubiquitin-like polypeptides. In this study, the recombinant protein SUMO from A. flavus was cloned and expressed in E. coli BL21 (DE3). The protein was purified by nickel column affinity chromatography method and identified by mass spectrometry with molar mass was 10296 Da. The yield of recombinant protein was > 90% pure. The SUMO protein was immunized into BALB/c mice, and its potency was measured by western blot. The predicted superposition model of SUMO protein was analyzed by ITASEER server. These results indicated that SUMO proteins and its polyclonal antibody might provide scientific basis to study the SUMOylation in A. flavus.

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