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  • 1
    Electronic Resource
    Electronic Resource
    The yeast nuclear gene MRP-L13 codes for a protein of the large subunit of the mitochondrial ribosome (1994)
    Springer
    Current genetics 26 (1994), S. 8-14 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Nuclear gene ; Mitochondria ; Mitochondrial ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear gene MRP-L13 of Saccharomyces cerevisiae, which codes for the mitochondrial ribosomal protein YmL13, has been cloned and characterized. It is a single-copy gene residing on chromosome XI. Its nucleotide sequence was found to be identical to that of the previously reported ORF YK105. A comparison of the predicted protein sequence of the MRP-L13 gene product and the actual N-terminal amino-acid sequence of the isolated YmL13 protein indicated that the mature protein is preceded by a mitochondrial signal peptide of 86 amino-acid residues, which is the longest among all known mitochondrial ribosomal proteins of S. cerevisiae. No sequence similarity was found to any other ribosomal protein in the current databases. The transcription of MRP-L13 was found to be repressed in the presence of glucose. Its protein product is not strictly essential for mitochondrial functions, but disruption of the gene by insertion of LEU2 noticeably affected cellular growth on non-fermentable carbon sources.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326298
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  • 2
    Electronic Resource
    Electronic Resource
    The substrate specificity of uptake2 in the rat heart (1984)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 328 (1984), S. 164-173 
    Details
    ISSN: 1432-1912
    Keywords: Extraneuronal uptake ; Rat heart ; Catecholamines ; Stereoselectivity ; Substrate specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Experiments were carried out with hearts isolated from reserpine- and pargyline-pretreated rats; both noradrenaline-metabolizing enzymes and uptake1 were inhibited. Initial rates of extraneuronal uptake were measured after perfusion lasting for 2 min, either in the absence or in the presence of 100 μmol/l O-methyl-isoprenaline, a potent inhibitor of uptake2. 1. The ID50 (i.e., the concentration of unlabelled substance that halves the rate of uptake of a tracer concentration of 3H-(±)-isoprenaline) was determined for a variety of agents. Two types of stereoselective preference of (-)-isomers were observed: for isoprenaline and adrenaline (but not for noradrenaline)-and also for dobutamine. 2. The stereoselective preference for the (-)-isomers of isoprenaline and adrenaline is also evident from fluorimetric determination of initial rates of uptake of unlabelled isomers. 3. Experiments with various tritiated compounds indicate that uptake2 has a broad substrate spectrum: uptake2 is not restricted to 3H-catecholamines and 3H-phenethylamines, but extends to resorcinols (3H-orciprenaline), imidazoline derivatives (3H-clonidine), 3H-histamine and 3H-5-hydroxytryptamine (3H-5-HT). 4. Determinations of the V max of uptake2 revealed a correlation between the ID50 and the V max: the higher the ID50, the higher the V max. 5. These results indicate that uptake2 is a carrier-mediated process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00512067
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  • 3
    Electronic Resource
    Electronic Resource
    The handling of five amines by the extraneuronal deaminating system of the rat heart (1988)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 337 (1988), S. 159-163 
    Details
    ISSN: 1432-1912
    Keywords: Extraneuronal monoamine oxidase ; Uptake2 ; Rat heart ; Extraneuronal deaminating system ; Catecholamines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The handling of five amines by the extraneuronal deaminating system was studied in perfused hearts of rats (pretreated with reserpine; COMT and neuronal uptake inhibited). Hearts were perfused with 50 nmol/l 3H-noradrenaline for 30 min, in the presence of increasing concentrations of unlabelled (−)-adrenaline, (−)-noradrenaline, dopamine, tyramine and 5-HT. IC50's were determined as those concentrations of unlabelled amines which halved the steady-state rate of deamination of 3H-noradrenaline. After correction for changes in the tissue/medium ratio for 3H-noradrenaline, “half-saturating outside concentrations” were obtained. They increased in the order (−)-adrenaline (15 μmol/l) — tyramine — dopamine — noradrenaline —5-HT (53 μmol/l). The V max for extraneuronal deamination was determined for 3H-(−)-adrenaline, 3H-(−)-noradrenaline and 3H-dopamine, as well as (by HPLC and electrochemical detection) for tyramine and 5-HT. It was low for (−)-adrenaline, intermediate for (−)-noradrenaline, dopamine and 5-HT, high for tyramine. For the three catecholamines the half-saturating outside concentrations of the extraneuronal deaminating system clearly exceeded those for the extraneuronal O-methylating system of the same organ (see Grohmann and Trendelenburg 1985), although the two enzymes appear to co-exist in the same cells, so that the same transport system is involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169243
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  • 4
    Electronic Resource
    Electronic Resource
    The 28.5-kDa iron-sulfur protein of mitochondrial complex I is encoded in the nucleus in plants (1997)
    Springer
    Molecular genetics and genomics 253 (1997), S. 448-454 
    Details
    ISSN: 1617-4623
    Keywords: Key words Plant mitochondria ; Iron-sulfur protein ; Complex I ; Nuclear gene ; Introns
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The intrinsic 28.5-kDa iron-sulfur protein of complex I in the mitochondrial respiratory chain is encoded in the nucleus in animals and fungi, but specified by a mitochondrial gene in trypanosomes. In plants, the homologous protein is now found to be encoded by a single-copy nuclear gene in Arabidopsis thaliana and by two nuclear genes in potato. The cysteine motifs involved in binding two iron-sulfur clusters are conserved in the plant protein sequences. The locations of the seven introns, with sizes between 60 and 1700 nucleotides, are identical in the A. thaliana and the two potato genes, while their primary sequences diverge considerably. The A+T contents of the intron sequences range between 61% and 73%, as is characteristic for dicot plants, but are in some instances not higher than in the adjacent exons. Here, differences in T content may instead serve to discriminate exons and introns. In potato, both genes are expressed, with the highest levels found in flowers. Sequence similarities between the homologous nuclear and mitochondrial genes indicate that the nuclear forms in animals and plants originate from the endosymbiont genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050342
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    Paper (German National Licenses)
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