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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Immunochemical properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli.

The preparation, characterization, and purification of antibody against the membrane-bound D-lactate dehydrogenase solubilized and purified from Escherichia coli ML 308-225 are described. The antibody is highly specific for the flavin-linked D-lactate dehydrogenase, and incubation of the enzyme with antiserum results in marked inhibition of enzymatic activity. By means of a radioimmune assay, it is demonstrated that membrane vesicles prepared from E. coli ML 308-225dld-3 contain catalytically inactive material which cross-reacts with native D-lactate dehydrogenase. In the following paper, the effects of this antiserum on D-lactate dehydrogenase activity and D-lactate-dependent active transport in native and reconstituted membrane vesicles are examined.[1]

References

  1. Immunochemical properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. Short, S.A., Kaback, H.R., Hawkins, T., Kohn, L.D. J. Biol. Chem. (1975) [Pubmed]
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