Molecular cloning, purification and immunogenicity of recombinant Brucella abortus 544 malate dehydrogenase protein

布鲁氏菌544重组苹果酸脱氢酶蛋白的分子克隆、纯化和免疫原性研究

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Abstract

The Brucella mdh gene was successfully cloned and expressed in E. coli. The purified recombinant malate dehydrogenase protein (rMDH) was reactive to Brucella-positive bovine serum in the early stage, but not reactive in the middle or late stage, and was reactive to Brucella-positive mouse serum in the late stage, but not in the early or middle stage of infection. In addition, rMDH did not react with Brucella-negative bovine or mouse sera. These results suggest that rMDH has the potential for use as a specific antigen in serological diagnosis for early detection of bovine brucellosis.

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