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  • 1
    Electronic Resource
    Electronic Resource
    Oil shale retort water ammonia determination by titrimetry, phenate colorimetry, enzymatic analysis, and chromatographic fractionation/chemiluminescence (1986)
    s.l. : American Chemical Society
    Analytical chemistry 58 (1986), S. 1556-1561 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00298a064
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  • 2
    Electronic Resource
    Electronic Resource
    Sampling for Toxic Contaminants in Ground Water (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Ground water monitoring & remediation 6 (1986), S. 0 
    Details
    ISSN: 1745-6592
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geosciences
    Notes: In this paper, we relate recent developments in ground water sampling techniques to the practical application of sampling for toxic contaminants in ground water. We address the choices that must be made in choosing equipment for a particular project by going through a step-by-step procedure for collecting a ground water sample from a typical monitoring well. Ground water sampling topics that are discussed include: choice of equipment for purging and sampling a well, monitoring for purged ground water indicators and quality assurance/quality control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-6592.1986.tb01241.x
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  • 3
    Electronic Resource
    Electronic Resource
    VII.—A NEW SPECIFIC GRAVITY BOTTLE. (1881)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 3 (1881), S. 26-26 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja02153a004
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  • 4
    Electronic Resource
    Electronic Resource
    Bioinformatics needs a software archive (2004)
    [s.l.] : Nature Publishing Group
    Nature 429 (2004), S. 241-241 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sir In February 2003 the US National Institutes of Health (NIH) released a statement on its data-sharing policy, in which it strengthened its commitment to free exchange of final research data produced by public funds (see Nature 421, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/429241b
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  • 5
    Electronic Resource
    Electronic Resource
    Darkness and antibiotics increase the steady-state transcripts of the elongation factor gene (tuf) inChlamydomonas reinhardtii (1988)
    Springer
    Current genetics 14 (1988), S. 119-126 
    Details
    ISSN: 1432-0983
    Keywords: Chloroplast ; Elongation ; Factor/SteadyState ; Transcripts/ Light ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A plasmid library of chloroplast (Cp) DNA fromChlamydomonas reinhardtii was used to screen for transcripts which respond to light. A transcript of R03, a 1,300 byEcoRI fragment, was identified as a message which accumulates in darkness. The transcribed region of R03 showed extensive sequence homology with theEscherichia coli elongation factor gene,tufA. A genespecific probe was constructed. Northern blots were used to study the extent and kinetics of accumulation of this transcript in darkness and in the presence of antibiotic inhibitors of Cp ribosomes. For comparison, the effects of darkness and antibiotics on the steady state levels ofpsbA, rbeL, and 16S rRNA were also studied. We conclude that thetuf transcript shows the greatest increase in darkness and in the presence of antibiotics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00569335
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  • 6
    Electronic Resource
    Electronic Resource
    Animal lib and racial bigotry (1992)
    [s.l.] : Nature Publishing Group
    Nature 356 (1992), S. 651-651 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR - David Wolpert1 equates animal research with racial bigotry. But the rhetoric of animal rights groups, particularly antivivisectionists, is disturbingly similar to the rhetoric of groups that promote racial violence. At the centre of antivivisectionism is a core of extreme cynicism and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/356651a0
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  • 7
    Electronic Resource
    Electronic Resource
    Sale of public databases puts biological data at risk (2005)
    [s.l.] : Nature Publishing Group
    Nature 435 (2005), S. 1028-1028 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sir For many years, biology journals have expected data to be submitted to public databases before publication. For example, requiring a GDB accession number (or D-segment identifier) before publication of human gene mapping results enhanced the growth of GenBank. When these ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/4351028c
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  • 8
    Electronic Resource
    Electronic Resource
    Soybean DapA mutations encoding lysine-insensitive dihydrodipicolinate synthase (1997)
    Springer
    Plant molecular biology 33 (1997), S. 931-933 
    Details
    ISSN: 1573-5028
    Keywords: DapA ; dihydrodipicolinate synthase ; Glycine max ; lysine ; soybean
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In plants, the rate-limiting step in the pathway for lysine synthesis is catalyzed by the enzyme dihydrodipicolinate synthase (DS), which is encoded by the DapA gene. We previously cloned the soybean (Glycine max cv. Century) DapA gene in Escherichia coli to express functional soybean DS protein. Like the wild-type soybean DS enzyme, the DS activity encoded by the cloned gene was extremely sensitive to feedback inhibition by micromolar concentrations of lysine. Three mutants of the soybean DapA gene were constructed using PCR: one with a single amino acid substitution at codon 104, another with a single amino acid substitution at codon 112, and a mutant containing both modifications. When expressed in E. coli, the mutant DS activities were insensitive to lysine at concentrations up to 1 mM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005766330149
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  • 9
    Electronic Resource
    Electronic Resource
    Posttranscriptional accumulation of chloroplast tufA (elongation factor gene) mRNA during chloroplast development in Chlamydomonas reinhardtii (1993)
    Springer
    Plant molecular biology 23 (1993), S. 87-96 
    Details
    ISSN: 1573-5028
    Keywords: Chlamydomonas ; chloroplast ; mRNA ; tufA/y-1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Light induces chloroplast (Cp) differentiation in dark-grown y-1 strains of Chlamydomonas reinhardtii. Slot blot analysis was used to quantitate tufA, psbA, psbK, rbcL, and 16S rRNA transcript accumulation and transcription during Cp differentiation. When etiolated cc-125 y-1 cells were illuminated for 5 h, a 1710 bp tufA mRNA accumulated up to 5-fold while the psbA, rbcL, and 16S rRNA transcripts accumulated less than 1.5-fold. The tufA gene encodes translational elongation factor EF-Tu. The light-induced accumulation of tufA mRNA did not occur in cc-1931, a strain that does not become etiolated in darkness. Pulse labelling was used to measure the transcription of Cp transcripts during tufA mRNA accumulation, and no detectable change in tufA transcription was observed. These results imply that the half life of the tufA transcript increases during the greening process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00021422
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning and expression of the soybean DapA gene encoding dihydrodipicolinate synthase (1994)
    Springer
    Plant molecular biology 26 (1994), S. 989-993 
    Details
    ISSN: 1573-5028
    Keywords: DapA ; dihydrodipicolinate synthase ; glycine max ; lysine ; soybean
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The rate-limiting step in the pathway for lysine synthesis in plants is catalyzed by the enzyme dihydrodipicolinate synthase (DS). We have cloned the portion of the soybean (Glycine max cv. Century) DapA cDNA that encodes the mature DS protein. Expression of the cloned soybean cDNA as a lacZ fusion protein was selected in a dapA - Escherichia coli auxotroph. The DS activity of the fusion protein was characterized in E. coli extracts. The DS activity of the fusion protein was inhibited by lysine concentrations that also inhibited native soybean DS, while E. coli DS activity was much less sensitive to inhibition by lysine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028865
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