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  • Articles: DFG German National Licenses  (4)
  • 1975-1979  (4)
Source
  • Articles: DFG German National Licenses  (4)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 14 (1977), S. 101-108 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Rat liver mitochondrial polyribosomes were isolated free from cytoplasmic ribonucleoprotein contaminations in a number of criteria (sedimentation and buoyant density patterns, ribosomal RNA composition). Heterogeneous poly A containing RNA from mitochondrial polysomes was purified by two-stage cellulose chromatography. This RNA was in vitro labelled with125I up to specific activity ~106–107 cts.min−1.µg −1 and used for hybridization experiments with separate complementary strands of mitochondrial DNA and nuclear DNA fragments. The proportions of mitochondrial poly A containing RNA that is complementary to heavy and light strands of mtDNA were respectively 31.5% and 8.3%. Besides, a significant RNA fraction was complementary to unique sequences of nuclear DNA (2–3 copies per haploid genome). The hybrids that were formed possessed a high Tm indicative of a perfect base pairing. A dual intracellular origin of mitochondrial messenger RNA is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 14 (1977), S. 91-96 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Some properties of a submitochondrial cell-free system for protein synthesis are described. The system was prepared from rat liver mitochondria lysed with Triton X-100, and the lysate was characterized by a linear rate of [14C]amino acid incorporation for 15–20 min with subsequent decline in activity. The incorporation reaction was inhibited by chloramphenicol and was in-sensitive to cycloheximide. Poly(U) addition stimulated [14C]phenylalanine incorporation by the preincubated submitochondrial system. Upon the addition of 7.5S mRNA that was iso-lated from mitochondria the major translation product was identified as a hydrophobic poly-peptide which in some properties (solubility in chloroform-methanol mixture) was similar to one of polypeptides synthesized by the sub-mitochondrial system on endogeneous mRNAs.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4927
    Keywords: Wilson's disease ; ceruloplasmin ; genetic defect in protein synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Comparative immunochemical analysis of ceruloplasmin-synthesizing polyribosomes in liver biopsies from control subjects and homozygous carriers of the Wilson's mutation was performed. According to I 125 -antibody binding data, the amount of ceruloplasmin-forming liver polysomes in patients with Wilson's disease was 10–20 times lower than that in non-Wilson patients. Correspondingly, the pulse labeling of ceruloplasmin polypeptides was decreased severalfold in the cell-free liver preparations from patients with Wilson's disease.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Partially purified ceruloplasmin mRNA was isolated using indirect immunoprecipitation of rat liver polysomes and poly(U)-Sepharose chromatography of polysomal RNA. This RNA programmed the synthesis of ceruloplasmin polypeptides in a cell-free system from mitochondria. Immunochemical analysis of the translation products revealed a 40-fold enrichment of the ceruloplasmin mRNA activity. The purified ceruloplasmin mRNA migrated as a major homogeneous component with an apparent molecular weight about 1×106 daltons in polyacrylamide gels containing sodium dodecyl sulfate. The immunoprecipitated products of the cell-free translation had molecular weights in the range 4.5–5.4×104 daltons as estimated by gel-electrophoresis under denaturating conditions. These values approach the weight of the half-molecule of native ceruloplasmin.
    Type of Medium: Electronic Resource
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