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  • 1
    Publication Date: 2014-03-29
    Description: Photosynthesis in the surface ocean produces approximately 100 gigatonnes of organic carbon per year, of which 5 to 15 per cent is exported to the deep ocean. The rate at which the sinking carbon is converted into carbon dioxide by heterotrophic organisms at depth is important in controlling oceanic carbon storage. It remains uncertain, however, to what extent surface ocean carbon supply meets the demand of water-column biota; the discrepancy between known carbon sources and sinks is as much as two orders of magnitude. Here we present field measurements, respiration rate estimates and a steady-state model that allow us to balance carbon sources and sinks to within observational uncertainties at the Porcupine Abyssal Plain site in the eastern North Atlantic Ocean. We find that prokaryotes are responsible for 70 to 92 per cent of the estimated remineralization in the twilight zone (depths of 50 to 1,000 metres) despite the fact that much of the organic carbon is exported in the form of large, fast-sinking particles accessible to larger zooplankton. We suggest that this occurs because zooplankton fragment and ingest half of the fast-sinking particles, of which more than 30 per cent may be released as suspended and slowly sinking matter, stimulating the deep-ocean microbial loop. The synergy between microbes and zooplankton in the twilight zone is important to our understanding of the processes controlling the oceanic carbon sink.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giering, Sarah L C -- Sanders, Richard -- Lampitt, Richard S -- Anderson, Thomas R -- Tamburini, Christian -- Boutrif, Mehdi -- Zubkov, Mikhail V -- Marsay, Chris M -- Henson, Stephanie A -- Saw, Kevin -- Cook, Kathryn -- Mayor, Daniel J -- England -- Nature. 2014 Mar 27;507(7493):480-3. doi: 10.1038/nature13123. Epub 2014 Mar 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] National Oceanography Centre, University of Southampton, Waterfront Campus, European Way, Southampton SO14 3ZH, UK [2] Ocean and Earth Sciences, University of Southampton, European Way, Southampton SO14 3ZH, UK [3] Institute of Biological and Environmental Sciences, Oceanlab, University of Aberdeen, Newburgh AB41 6AA, UK. ; National Oceanography Centre, University of Southampton, Waterfront Campus, European Way, Southampton SO14 3ZH, UK. ; Aix-Marseille Universite, Universite de Toulon, CNRS/INSU, IRD, MIO, UM 110, 13288 Marseille Cedex 09, France. ; 1] Ocean and Earth Sciences, University of Southampton, European Way, Southampton SO14 3ZH, UK [2] Department of Earth and Ocean Sciences, University of South Carolina, Columbia, South Carolina 29208, USA. ; Marine Laboratory, Marine Scotland Science, Scottish Government, PO Box 101, 375 Victoria Road, Aberdeen AB11 9DB, UK. ; Institute of Biological and Environmental Sciences, Oceanlab, University of Aberdeen, Newburgh AB41 6AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24670767" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquatic Organisms/*metabolism ; Atlantic Ocean ; Biota ; Carbon/*metabolism ; *Carbon Cycle ; Carbon Dioxide/metabolism ; Carbon Sequestration ; Cell Respiration ; Food Chain ; Observation ; *Seawater/chemistry/microbiology ; Uncertainty ; Zooplankton/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
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    In:  EPIC3Ecology, 85, pp. 1193-1202
    Publication Date: 2019-07-17
    Repository Name: EPIC Alfred Wegener Institut
    Type: Article , isiRev
    Format: application/pdf
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 33 (1981), S. 261-267 
    ISSN: 1432-0827
    Keywords: Acid phosphatases ; Acid phosphoprotein phosphatases ; Bone phosphatases ; Enzyme purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Studies were designed to examine the effects of isotonic sucrose and hypertonic KCl on the extraction and properties of phosphatases (acid optima) from long bones of suckling rats. Low-speed supernatants (S) of homogenates in sucrose were dialyzed against sucrose or deionized H2O. Free enzyme was recovered from both retentates by ultracentrifugation before (S1) or after sequential treatment with KCl and Triton X-100 (S2), protamine (S3), and a final dialysis (S4). Activity was measured withp-nitrophenylphosphate (p-NPP), β-glycerophosphate (β-GP), ATP, and casein. S was evaluated for latent enzyme with hypertonic KCl and classic lysing methods. Fractionation of activity in final extracts was accomplished with CM-52 cellulose or electrophoresis. Results showed that: (a) sucrose did not alter the types or properties of enzymes extracted, but did decrease yield of activities; (b) activity in S was increased approximately 20% by lysing methods, 80% by hypertonic KCl, and was unstable unless salt and detergent were present; and (c) chromatography or electrophoresis of S4 resolved only two enzymes: a tartrate-sensitive phosphomonoesterase (E1) responsible for 15% of the total activity in S, and a tartrate-insensitive enzyme (E2) which accounted for 85% of the activity, was unstable in isotonic medium, had high affinity for ATP andp-NPP, and had low affinity for casein and β-GP. It is concluded that sucrose is not necessary for the isolation of total bone acid phosphatase activity, that hypertonic KCl does not negatively affect the properties of the enzymes isolated, and that E1 and E2 show different latencies.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 24 (1977), S. 187-190 
    ISSN: 1432-0827
    Keywords: Column chromatography ; Acidβ-glycerophosphatase ; Acid inorganic pyrophosphatase ; Acid p-nitrophenylphosphatase ; Bone phosphatases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Extracts of tibiae of suckling rats were prepared with 0.3 M KCl containing 0.1% Triton X-100 and were chromatographed with CM-52 cellulose. Most of the acid phosphatase activity determined with p-nitrophenylphosphate (p-NPP) was bound to the cellulose and could be eluted with a sodium acetate buffer gradient in 2 distinct peaks. The major peak, E2, was bound strongly to the cellulose and showed high activity with p-NPP and inorganic pyrophosphate (P-Pi), but only slight activity withβ-glycerophosphate (β-GP) and was unaffected by tartrate. The minor peak, E1, was weakly bound to the adsorbent, showed equal activity with p-NPP andβ-GP, but negligible activity with P-Pi and was completely inhibited by tartrate. These results support earlier evidence suggesting that bone contains at least 2 different acid phosphatases and that the more abundant enzyme may function as a pyrophosphatase.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 27 (1979), S. 219-226 
    ISSN: 1432-0827
    Keywords: Acid phosphatases ; Bone phosphatases ; ATPase ; Enzyme purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100. A high-speed supernatant was treated with protamine sulfate, dialyzed, and chromatographed on CM-52 cellulose. All of the acid phosphatase activity was eluted with a sodium acetate buffer and combined ionic strength-pH gradient into two peaks (E1 and E2). Both enzyme peaks were further purified with Sephadex G-200, which resulted in 700- and 1000-fold purification for E2 and E1, respectively. A total of 220 units (µmoles substrate/min) of E2 with a specific activity of 160 units/mg protein has been obtained in one run by this procedure. E1 has a high molecular weight (〉100,000) and shows preference for monophosphate ester substrates, is markedly inhibited by tartrate, and has a pH optimum near 5. E2 has a lower molecular weight (〈40,000) and shows negligible activity with monophosphate esters [except withp-nitrophenyl phosphate (p-NPP)], but high activity with ADP and ATP. E2 is unaffected by tartrate and shows a pH optimum near 6. Both enzymes are competitively inhibited by inorganic phosphate, and E2, but not E1, is markedly inhibited byp-chloromercuribenzoate. Withp-NPP as substrate, E1 and E2 have distinctly different values for Km. E1 appears similar to the high molecular weight acid phosphatases of soft tissues. However, E2 appears to differ from the low molecular weight phosphatases in soft tissues with regard to substrate specificity.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 34 (1982), S. 54-58 
    ISSN: 1432-0827
    Keywords: Acid phosphatases ; Acid phosphoprotein phosphatases ; Bone phosphatases ; Ferrous iron ; Ascorbic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The effect of ferrous iron (Fe2+) and the reducing agents cysteine, dithiothreitol, and especially ascorbate on acid phosphatase activity was determined in vitro. Activity was extracted from homogenates of suckling rat tibia and femur with hypertonic KCl and Triton X-100, treated with protamine to remove interfering macromolecules, and dialyzed. Tartrate-sensitive and tartrate-resistant activity were separated and partially purified by cation exchange chromatography. At optimum dosage levels, Fe2+ was 100 times more potent than reducing agents in stimulating activity. Hypertonic KCl facilitated the effects of all agents. Fe2+ had no effect on tartrate-sensitive activity (E1), but specifically stimulated the hydrolysis ofβ-glycerophosphate, casein, and especially ATP andp-nitrophenylphosphate (p-NPP) by tartrate-resistant enzyme (E2); other divalent cations were either inhibitory or ineffective over a concentration range of 10−5 to 10−2M. Stimulation of E2 was detectable at 10−6M Fe2+, and the effect was synergistically increased by 10−3M ascorbate. E2 was stimulated maximally at 10−4M Fe2+ + 10−3M ascorbate, but at these concentrations their combined effects were additive. Both stimulated and unstimulated enzyme had identical pH optima (5.8), but the activity of the stimulated enzyme declined more slowly at higher pH values. Hypertonic KCl, Fe2+, or ascorbate reduced one-fourth to one-half the Km of activity withp-NPP substrate, which suggested a direct effect of these substances on E2. It is postulated the Fe2+ may interact with sulfhydryl groups in E2, and that reducing agents and KCl may facilitate this action by (a) maintaining the enzyme in an optimal conformational state, and (b) keeping iron reduced as Fe2+.
    Type of Medium: Electronic Resource
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  • 7
    Publication Date: 2015-11-26
    Description: The direct-drive, laser-based approach to inertial confinement fusion (ICF) is reviewed from its inception following the demonstration of the first laser to its implementation on the present generation of high-power lasers. The review focuses on the evolution of scientific understanding gained from target-physics experiments in many areas, identifying problems that were demonstrated and the solutions implemented. The review starts with the basic understanding of laser–plasma interactions that was obtained before the declassification of laser-induced compression in the early 1970s and continues with the compression experiments using infrared lasers in the late 1970s that produced thermonuclear neutrons. The problem of suprathermal electrons and the target preheat that they caused, associated with the infrared laser wavelength, led to lasers being built after 1980 to operate at shorter wavelengths, especially 0.35  μ m—the third harmonic of the Nd:glass laser—and 0.248  μ m (the KrF gas laser). The main physics areas relevant to direct drive are reviewed. The primary absorption mechanism at short wavelengths is classical inverse bremsstrahlung. Nonuniformities imprinted on the target by laser irradiation have been addressed by the development of a number of beam-smoothing techniques and imprint-mitigation strategies. The effects of hydrodynamic instabilities are mitigated by a combination of imprint reduction and target designs that minimize the instability growth rates. Several coronal plasma physics processes are reviewed. The two-plasmon–decay instability, stimulated Brillouin scattering (together with cross-beam energy transfer), and (possibly) stimulated Raman scattering are identified as potential concerns, placing constraints on the laser intensities used in target designs, while other processes (self-focusing and filamentation, the parametric decay instability, and magnetic fields), once considered important, are now of lesser concern for mainline direct-drive target concepts. Filamentation is largely suppressed by beam smoothing. Thermal transport modeling, important to the interpretation of experiments and to target design, has been found to be nonlocal in nature. Advances in shock timing and equation-of-state measurements relevant to direct-drive ICF are reported. Room-temperature implosions have provided an increased understanding of the importance of stability and uniformity. The evolution of cryogenic implosion capabilities, leading to an extensive series carried out on the 60-beam OMEGA laser [Boehly et al. , Opt. Commun. 133 , 495 (1997)], is reviewed together with major advances in cryogenic target formation. A polar-drive concept has been developed that will enable direct-drive–ignition experiments to be performed on the National Ignition Facility [Haynam et al. , Appl. Opt. 46 (16), 3276 (2007)]. The advantages offered by the alternative approaches of fast ignition and shock ignition and the issues associated with these concepts are described. The lessons learned from target-physics and implosion experiments are taken into account in ignition and high-gain target designs for laser wavelengths of 1/3  μ m and 1/4  μ m. Substantial advances in direct-drive inertial fusion reactor concepts are reviewed. Overall, the progress in scientific understanding over the past five decades has been enormous, to the point that inertial fusion energy using direct drive shows significant promise as a future environmentally attractive energy source.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
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  • 10
    Publication Date: 2005-07-01
    Print ISSN: 0011-183X
    Electronic ISSN: 1435-0653
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Published by Wiley
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