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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 81 (1959), S. 3483-3484 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 49 (1987), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Gene cha-1 · unc-17 of the nematode Caenorhabditis elegans is a complex gene, consisting of at least two complementation groups. One part (cha-1 region) of the gene encodes the enzyme choline acetyltransferase (ChAT), but the function of the other part (unc-17 region) is still unclear. We measured the ChAT activity and ACh levels of the cha-1 and unc-17 complex gene mutants. We show here that alterations in ACh levels, rather than the ChAT activity, reflect abnormal phenotypes accompanying cha-1 · unc-17 mutations, that is, the decreased ACh levels in cha-1 mutations and abnormal accumulation in unc-17 mutations. Our results suggest that the unc-17 region may encode functions necessary for storage and/or release of ACh at the presynaptic level.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 2991-3003 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Although a shift in nutritinal conditins brings about transient unbalanced growth in normally grown Escherichia coli, a shift in temperature without changing the nutritional conditions results in immediate adaptation to the new conditions. However, when a medium contained an insufficient amount of nutrient, such as glucose, a temperature shift caused a lag time in temperature shiftup was primarily determined by the postshift temperature. These situatins were quite similar to those observed in nutrient shiftup, but a growth profile during the lag time was more distorted than that found in the nutrient shiftup. The transient unbalanced growth appeared to be caused by a difference in physiological states of bacteria, as expressed by macromolecule content per cell characterized by the pre and postshift environments, and was capable of expressing theoretically its profile and duration according to the model of Cooper and Helmstetter. On the other hand, the shiftdown in temperature in the presence of a limiting concentration of glucose caused extraordinarily long lag time, and transient cessation of cell division during that period. This response was unable to explain by the Cooper and Helmstetter model. In contrast to the temperature shiftup, the duration of lag time in the shiftdown was expresed as functions of the poshift temperature and the difference in physiological states of the pre- and postshift environments.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Keywords: Replication origin ; Gel shift assay ; Nuclear protein ; Single stranded DNA ; DNA-binding protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To study the mechanism of initiation of eukaryotic chromosomal replication, we examined protein factors interacting with the ARS1 region located near the centromere of chromosome IV in Saccharomyces cerevisiae. Using the gel shift assay, we found protein factor(s) which specifically bound to the T-rich strand of the region containing the core consensus and its flanking sequences in ARS1, but not to the opposite strand. We designated this factor ATS (ARS1, T-rich strand-binding factor(s)). Similar specific complexes were also detected with oligonucleotide probes specific for the H4 or C2G1 ARS. As we have previously identified another binding factor, we conclude that at least two factors bind to the single-stranded ARS1 sequence.
    Type of Medium: Electronic Resource
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