Hydrothermal Experiments with Protonated Benzylamines Provide Predictions of Temperature-Dependent Deamination Rates for Geochemical Modeling

Author(s):  
Kirtland J. Robinson ◽  
Ian R. Gould ◽  
Hilairy E. Hartnett ◽  
Lynda B. Williams ◽  
Everett L. Shock
2019 ◽  
Vol 104 (7) ◽  
pp. 936-948 ◽  
Author(s):  
Maxim Gavrilenko ◽  
Michael Krawczynski ◽  
Philipp Ruprecht ◽  
Wenlu Li ◽  
Jeffrey G. Catalano

AbstractHere we present a study on the quenchability of hydrous mafic melts. We show via hydrothermal experiments that the ability to quench a mafic hydrous melt to a homogeneous glass at cooling rates relevant to natural samples has a limit of no more than 9 ± 1 wt% of dissolved H2O in the melt. We performed supra-liquidus experiments on a mafic starting composition at 1–1.5 GPa spanning H2O-undersaturated to H2O-saturated conditions (from ~1 to ~21 wt%). After dissolving H2O and equilibrating, the hydrous mafic melt experiments were quenched. Quenching rates of 20 to 90 K/s at the glass transition temperature were achieved, and some experiments were allowed to decompress from thermal contraction while others were held at an isobaric condition during quench. We found that quenching of a hydrous melt to a homogeneous glass at quench rates comparable to natural conditions is possible at water contents up to 6 wt%. Melts containing 6–9 wt% of H2O are partially quenched to a glass, and always contain significant fractions of quench crystals and glass alteration/devitrification products. Experiments with water contents greater than 9 wt% have no optically clear glass after quench and result in fine-grained mixtures of alteration/devitrification products (minerals and amorphous materials). Our limit of 9 ± 1 wt% agrees well with the maximum of dissolved H2O contents found in natural glassy melt inclusions (8.5 wt% H2O). Other techniques for estimating pre-eruptive dissolved H2O content using petrologic and geochemical modeling have been used to argue that some arc magmas are as hydrous as 16 wt% H2O. Thus, our results raise the question of whether the observed record of glassy melt inclusions has an upper limit that is partially controlled by the quenching process. This potentially leads to underestimating the maximum amount of H2O recycled at arcs when results from glassy melt inclusions are predominantly used to estimate water fluxes from the mantle.


Author(s):  
T.E. Pratt ◽  
R.W. Vook

(111) oriented thin monocrystalline Ni films have been prepared by vacuum evaporation and examined by transmission electron microscopy and electron diffraction. In high vacuum, at room temperature, a layer of NaCl was first evaporated onto a freshly air-cleaved muscovite substrate clamped to a copper block with attached heater and thermocouple. Then, at various substrate temperatures, with other parameters held within a narrow range, Ni was evaporated from a tungsten filament. It had been shown previously that similar procedures would yield monocrystalline films of CU, Ag, and Au.For the films examined with respect to temperature dependent effects, typical deposition parameters were: Ni film thickness, 500-800 A; Ni deposition rate, 10 A/sec.; residual pressure, 10-6 torr; NaCl film thickness, 250 A; and NaCl deposition rate, 10 A/sec. Some additional evaporations involved higher deposition rates and lower film thicknesses.Monocrystalline films were obtained with substrate temperatures above 500° C. Below 450° C, the films were polycrystalline with a strong (111) preferred orientation.


1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.


1996 ◽  
Vol 75 (03) ◽  
pp. 515-519 ◽  
Author(s):  
Mark J Post ◽  
Anke N de Graaf-Bos ◽  
George Posthuma ◽  
Philip G de Groot ◽  
Jan J Sixma ◽  
...  

Summary Purpose. Thermal angioplasty alters the thrombogenicity of the arterial wall. In previous studies, platelet adhesion was found to increase after heating human subendothelium to 55° C and decrease after heating to 90° C. In the present electron microscopic study, the mechanism of this temperature-dependent platelet adhesion to the heated arterial wall is elucidated by investigating temperature-dependent conformational changes of von Willebrand factor (vWF) and collagen types I and III and the binding of vWF to heated collagen. Methods. Purified vWF and/or collagen was applied to electron microscopic grids and heated by floating on a salt-solution of 37° C, 55° C or 90° C for 15 s. After incubation with a polyclonal antibody against vWF and incubation with protein A/gold, the grids were examined by electron microscopy. Results. At 37° C, vWF was coiled. At 55° C, vWF unfolded, whereas heating at 90° C caused a reduction in antigenicity. Collagen fibers heated to 37° C were 60.3 ± 3.1 nm wide. Heating to 55° C resulted in the unwinding of the fibers, increasing the width to 87.5 ± 8.2 nm (p < 0.01). Heating to 90° C resulted in denatured fibers with an enlarged width of 85.1 ± 6.1 nm (p < 0.05). Heating of collagen to 55° C resulted in an increased vWF binding as compared to collagen heated to 37° C or to 90° C. Incubation of collagen with vWF, prior to heating, resulted in a vWF binding after heating to 55° C that was similar to the 37° C binding and a decreased binding after 90° C. Conclusions. After 55° C heating, the von Willebrand factor molecule unfolds and collagen types I and III exhibit an increased adhesiveness for von Willebrand factor. Heating to 90° C denatures von Willebrand factor and collagen. The conformation changes of von Willebrand factor and its altered binding to collagen type I and III may explain the increased and decreased platelet adhesion to subendothelium after 55° C and 90° C heating, respectively.


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