ISSN:
1432-072X
Schlagwort(e):
Hydrogen-oxidation
;
NAD-linked hydrogenase
;
New Hox proteins
;
Hox B protein
;
linkage to soluble hydrogenase
;
Occurrance in hydrogen bacteria
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
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.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00406131
Permalink
