Mapping of the puh Messenger RNAs from Rhodospirillum rubrum
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چکیده
منابع مشابه
The succinic dehydrogenase from Rhodospirillum rubrum.
Succinic dehydrogenase has usually been associated with a macromolecular intracellular unit (mitochondria) whenever the enzyme has been isolated. In an ultracentrifugal analysis of the composition of extracts of various organisms, Schachman et al. (1952) found that Rhodospirillum rubrum yielded particles with a wide range of sedimentation constants. Succinic dehydrogenase has been demonstrated ...
متن کاملThe Structure of Rhodospirillum rubrum
Cells from serial cultures of R. rubrum, grown anaerobically in the light, were harvested at intervals from (1/2) to 15 days and sectioned for electron microscopy by conventional methods. Cells of this species possess a multilayered outer envelope, and the external cell surface is differentiated into ridges extending parallel or obliquely to the long axis of the cell. Cells from very young cult...
متن کاملWhole-genome shotgun optical mapping of Rhodospirillum rubrum.
Rhodospirillum rubrum is a phototrophic purple nonsulfur bacterium known for its unique and well-studied nitrogen fixation and carbon monoxide oxidation systems and as a source of hydrogen and biodegradable plastic production. To better understand this organism and to facilitate assembly of its sequence, three whole-genome restriction endonuclease maps (XbaI, NheI, and HindIII) of R. rubrum str...
متن کاملPhotosynthesis in Rhodospirillum rubrum
Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...
متن کاملCarbon monoxide dehydrogenase from Rhodospirillum rubrum.
The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis. In vitro, this enzyme catalyzed a two-electron oxidation of CO to form CO2 as the product. The reaction was dependent on the addition of an electron accept...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)81705-7