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. 1990 Sep;58(9):2935–2939. doi: 10.1128/iai.58.9.2935-2939.1990

Cloning, expression, and occurrence of the Brucella Cu-Zn superoxide dismutase.

B J Bricker 1, L B Tabatabai 1, B A Judge 1, B L Deyoe 1, J E Mayfield 1
PMCID: PMC313590  PMID: 2201639

Abstract

Recently, the complete amino acid sequence of a protein expressed in Escherichia coli from cloned Brucella abortus DNA was reported. On the basis of amino acid homology, this protein was identified as a copper-zinc superoxide dismutase (Cu-Zn SOD) (B. L. Beck, L. B. Tabatabai, and J. E. Mayfield, Biochemistry 29:372-376, 1990). We demonstrate in this paper that the sequenced protein is the same as the previously studied salt-extractable protein BCSP20. The plasmid-encoded protein expressed from recombinant E. coli is identical to the Brucella-derived BCSP20 in molecular mass, N-terminal amino acid sequence, and cross-reactivity with homologous and heterologous rabbit sera against either the recombinant gene product or the Brucella-derived protein. A survey of the expression of the Cu-Zn SOD protein in Brucella biovars representing all species was done by Western blotting (immunoblotting) using antisera raised against the recombinant E. coli-derived protein. With the exception of B. neotomae and B. suis biovar 2, the Cu-Zn SOD protein was detectable in all Brucella species and biovars tested, including eight biovars of B. abortus.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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