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  • 1
    Electronic Resource
    Electronic Resource
    Laboratory scale-up of two-stage laser chemistry separation of13C from CF2HCl (1985)
    Springer
    Applied physics 36 (1985), S. 63-75 
    Details
    ISSN: 1432-0649
    Keywords: 82.50 ; 33
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The laboratory scale-up of a two-stage laser enrichment process for carbon isotopes, involving infrared multiphoton dissociation of freon-22, is described. Unmodified commercial equipment and materials were used. An initial study of the effect of fluence, laser frequency, freon-22 pressure and pressure of argon, nitrogen and trifluoromethyl chloride was made in short irradiation cells (constant fluence) in order to define optimum process parameters. The process was then scaled to higher throughput in longer cells (1–5 m) in which compensation for beam-energy depletion by absorption was made by reduction in the beam area by focussing. From the scale-up experiments, measurements of yield and enrichment of the tetrafluoroethylene product gave demonstrated production rates. These, coupled with measurements of the absorption, allowed extrapolation to production rates assuming total utilization of the available output energy. Using a 100 W TEA CO2 laser (10 J, 10 Hz) we have demonstrated production rates of 0.20 g h−1 carbon-12 at 99.99% carbon-12, 11 mg h−1 carbon-13 at 72% carbon-13 and 2 kg per annum carbon-13 at 50%. Energy absorption measurements imply a capability to produce 3 kg per annum carbon-13 at over 95% carbon-13 in a two-stage process. The apparatus was used to produce gram quantities of carbon-13 depleted freon-22 (99.99% carbon-12). A comparison of the infrared multiphoton dissociation of this material with that of natural freon-22 (1.11% carbon-13) showed that under the conditions required to give selective dissociation of13CF2HCl that12CF2HCl was excited as a result of a dominantly radiative interaction and that collisional transfer from13CF2HCl molecules played a minor role.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00694692
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  • 2
    Electronic Resource
    Electronic Resource
    Stabilization of C5a receptor-G-protein interactions through ligand binding (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 380-388 
    Details
    ISSN: 0730-2312
    Keywords: C5a ; ligand binding ; G-protein ; second messenger systems ; neutrophils ; signal transduction ; receptor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Binding of biotin-C5a to the C5a receptor in membrane fragments followed by detergent solubilization and purification with streptavidin-agarose affinity chromatography resulted in the isolation of a receptor complex with associated G-proteins. In contrast, when receptor was detergent-solubilized in the absence of C5a and purified by affinity chromatography with Affigel-C5a, G-proteins did not copurify. Since the results indicate that receptor ligation stabilized the receptor-G-protein interaction to allow purification of the complex, the findings emphasize the dynamic nature of the C5a receptor-effector interactions. When biotin-C5a-ligated receptor was purified from a mouse cell line overexpressing recombinant human receptor, both Gialpha2 and Gialpha3 subunits copurified, confirming that multiple transducing systems are linked to the C5a receptor. The method of stabilization of receptor-transducer complexes offers the opportunity to further elaborate the interactions of the C5a receptor with diverse transducing elements and second messenger systems. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240550316
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  • 3
    Electronic Resource
    Electronic Resource
    Binding of glucocorticoid receptors to model DNA response elements (1991)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 47 (1991), S. 330-336 
    Details
    ISSN: 0730-2312
    Keywords: glucocorticoids ; steroid-receptor family ; steroid-hormone ; gene regulation ; transacting-factors ; mouse mammary tumor virus ; DNA-binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: DNA sequences were synthesized that contained the consensus 15-base pair glucocorticoid receptor binding site linked to flanking sequences of various lengths. Binding of these synthetic oligomers to glucocorticoid receptor, employing a reconstituted binding system with purified components, indicated that a minimal size of approximately 45 base pairs was necessary to bind the receptor optimally. Sequences containing multiple receptor binding sites competed more effectively for binding. These findings are consistent with recent demonstrations that multiple control elements act synergistically to affect transcriptional control by glucocorticoids and confirm that regions flanking the consensus GRE binding site are instrumental in optimizing binding interactions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240470407
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