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Identification of new peptides synthesized under the hydrogenase control system of Alcaligenes eutrophus

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Abstract

Total protein of Alcaligenes eutrophus was analyzed by two-dimensional protein map. Cells grown at 30° C expressed hydrogen-oxidizing (Hox) ability mediated by a soluble (Hos) and a particulate hydrogenase (Hop). Hox ability was not expressed at 37° C (HoxTs). The six subunits of the two hydrogenases were identified. Besides these six subunits eight peptides were not or hardly detected at 37° C. The mutant HF117 which expressed Hox ability at 37° C (HoxTr), formed the hydrogenase peptides and five of the eight peptides. These peptides designated B, C, E, F, and H were characterized by their isoelectric point and molecular mass (M r); their M r were 18 800, 45 400, 41 900, 39 400, and 40 600, respectively. The five peptides were not formed in regulatory Hox mutants, and not formed in mutants cured of plasmid pHG1, carrying the genetic information for hydrogenase formation. Strain HF160, carrying a Tn5 insertion in a gene essential for Hos expression specifically did not form the B-peptide. All peptides were found in the soluble fraction of cell extracts, the F-peptide was also detected in the particulate fraction. The function of the new Hox-peptides is presently unknown.

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Abbreviations

PAGE:

polyacrylamide gelelectrophoresis

SDS:

sodium dodecylsulfate

Hox:

hydrogen oxidizing ability

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Kärst, U., Friedrich, C.G. Identification of new peptides synthesized under the hydrogenase control system of Alcaligenes eutrophus . Arch. Microbiol. 147, 346–353 (1987). https://doi.org/10.1007/BF00406131

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