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.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000276:immunology; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000276:immunology; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007770:L-Lactate Dehydrogenase / Q000032:analysis* / Q000302:isolation & purification; D011092:Polyethylene Glycols; D011233:Precipitin Tests; D011817:Rabbits / Q000276:immunology; D011863:Radioimmunoassay
D011092:Polyethylene Glycols; D007770:L-Lactate Dehydrogenase