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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 118 (1978), S. 99-108 
    ISSN: 1432-072X
    Keywords: Chromatium vinosum ; Membrane differentiation ; Subchromatophore fractions ; Protein patterns ; Reaction center and light harvesting bacteriochlorophyll complexes ; Photophosphorylation ; Sulfide oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromatium vinosum, strain D, exhibits two extreme modifications of near infra-red absorption spectra when growing heterotrophically at temperatures either above or below 36.5° C. Chromatophores isolated from cells grown either at 33° C (33° C chromatophores) or 39° C (39° C chromatophores) were analyzed for structural and functional parameters. For this the following chromatophore subunits were solubilized and characterized; (i) a fraction absorbing maximally at 800 nm with shoulders at 820 and 850 nm when derived from 33° C chromatophores or absorbing at 800 nm and 850 nm when derived from 39° C chromatophores; (ii) reaction center-light harvesting bacteriochlorophyll complexes with identical spectra and ratios of reaction center to light harvesting bacteriochlorophyll (1:45); (iii) complexes containing cytochromes, (IV) reaction center bacteriochlorophyll complexes. Irrespective of their origins the fractions exhibited qualitatively identical protein patterns as analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Protein patterns of 33° C and 39° C chromatophores revealed an identical ratio of proteins of reaction centers to proteins of cytochrome preparations. But the ratio of proteins of reaction centers to proteins of light harvesting moieties was 1.9 times higher in 39° C chromatophores than in 33° C chromatophores. Correspondingly, the ratio of reaction center per total bacteriochlorophyll was 1.7 times higher in 39° C chromatophores (1:110) then in 33° C chromatophores (1:190). Activities of photophosphorylation were 0.73 and 0.56 μmoles of ATP per μmoles of total bacteriochlorophyll per min for 33° C and 39° C chromatophores, respectively. Activities of sulfide oxidation in the light by whole cells were 2.37 and 1.96 μmoles of sulfide per μmole of total bacteriochlorophyll per min for 33° C and 39° C cells. Accordingly, on a reaction center basis activities are significantly lower after growth of the organisms at 39° C than at 33° C. The data indicate that spectral changes in Chromatium vinosum represent changes in the ratio of reaction center to light harvesting bacteriochlorophyll accompanied by a variation of the absorption spectra of the latter bacteriochlorophyll moiety. Concomitantly, activities coupled to the photochemical apparatus were subjected to variations.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Drosophila recessive oncogene ; Mutations ; Molecular cloning ; Mobile elements ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Drosophila recessive oncogene lethal(2)giant larvae is located at the extreme left end of the second chromosome close to telomeric repetitive sequences. Of the 20 l(2)gl mutant alleles isolated from wild flies in widespread populations of the Soviet Union and California, all but two appear to represent large deletions which have removed the telomeric repetitive sequences and l(2)gl single copy sequences (Mechler et al. 1985). We have analyzed the structure of the two exceptions: the l(2)glGB52 mutation results from the insertion of a single transposable element of the B104 or roo family, whereas the more complex rearrangements of the l(2)glDV275 mutation consists of an 8 kb interstitial deletion whose breakpoints have become associated with a large transposed DNA fragment. Characterization of this fragment shows that it consists of B104 sequences flanked on one side by sequences originating from the chromosomal region 24D. Furthermore, we show that in both mutants normal transcription of the l(2)gl gene is abolished.
    Type of Medium: Electronic Resource
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