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. 2011 Nov 8;6(11):e27502. doi: 10.1371/journal.pone.0027502

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Floden et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Alignment of enolases from mouse, human, yeast and B. burgdorferi. Dark shaded residues indicate identity; light gray residues indicate similarity. Arrows indicate the 3 conserved residues that make up the enzymatic active site; stars indicate the three conserved residues required for binding the cofactor manganese. (B) A rabbit polyclonal antiserum directed against human enolase recognizes enolase from B. burgdorferi. Top panel: Western blot; Bottom panel: Coomassie-stained SDS-PAGE gel. Molecular weight markers are indicated on the left. Lane 1: fresh BSKII medium; Lane 2: spent BSKII medium from late-log phase cultures of B. burgdorferi; Lane 3: B. burgdorferi cell lysate; Lane 4: recombinant enolase from B. burgdorferi.