Immunochemical analysis of the membrane-bound succinate dehydrogenase of Escherichia coli

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The subunit mol. wt. of E. coli membrane-bound hydrogenase (I) of anaerobically grown cells was detd. by immunol. methods and the isolation and immunol. characterization of 2 E. coli mutants which lack I activity are reported. Crossed immunoelectrophoresis with antiserum against membrane vesicles contg. I gave a single, sym. arc for Triton X-100-solubilized membranes of wild-type E. coli strains A1002, EMG-2, and P4X. The polypeptide compn. of I, established by dodecyl sulfate-gel electrophoresis of immunoppts. recovered from 35S-labeled solubilized membranes, constituted a single radioactive band with a mol. wt. of 58,000. Multiple forms of I were not obsd. Two mutants lacking I activity were identified. These mutants phenotypically resembled hyd mutants described previously. Anal. indicated the gene order in these mutant strains (FD12 and FD10) to be: cysC-hyd-recA. The crossed immunoelectrophoresis patterns of Triton X-100-solubilized membranes from FD12 and FD10 against membrane vesicle antiserum were very similar to those of wild-type strains with the exception of lacking a precipitin arc for I. Furthermore, I was not detected in the lysates of these mutant strains. [on SciFinder(R)]




Jones, R. W., Kranz, R. G., & Gennis, R. B. (1982). Immunochemical analysis of the membrane-bound succinate dehydrogenase of Escherichia coli. FEBS Letters, 142(1), 81–87.

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