Quantifying microplastic particle transport and retention in an experimental flume environment

2021 ◽  
Author(s):  
Jan-Pascal Boos ◽  
Benjamin Gilfedder ◽  
Sven Frei
Keyword(s):  
Particle Transport ◽  
Solid Phase ◽  
River Sediments ◽  
Time Resolved ◽  
Fluvial Systems ◽  
Particle Mobility ◽  
Hyporheic Flow ◽  
Scale Experiment ◽  
Streambed Sediments ◽  
Experimental Flume

<p>Rivers and streams are the dominant transport vectors for microplastic (MP) input into marine environments. During transport, complex physicochemical interactions between particles, water and river sediments influence particle mobility and retention. The specific transport mechanisms of MP in fluvial systems are not yet fully understood, and the main reason lies in the limitation in reliable data derived from experimental analysis.</p><p>In our subproject of the ‘CRC 1357 Microplastics’, we investigate the hydrodynamic mechanisms that control the transport and retention behavior of MP in open channel flows and streambed sediments. In an experimental flume environment, we create realistic hydrodynamic and hyporheic flow conditions by using various porous media (e.g. glass beads or sand) and bedform structures (e.g. riffle-pool sequences, ripples and dunes), modelled from real stream systems.</p><p>The method developed here can quantitatively analyze the transport of pore-scale particles (1-40 µm) based on fluorometric techniques. Particle velocity distributions and particle transport are measured using Particle-Image-Velocimetry and Laser-Doppler-Velocimetry. With our setup, we can quantitatively investigate time-resolved MP transport and retention through the aqueous and solid phase in a flume scale experiment.</p>

Solute Segregation and Dynamics of Solid-Phase Crystallization In in and Sb-Implanted Silicon

1981 ◽  
Vol 4 ◽  
Author(s):  
J. Narayan ◽  
G. L. Olson ◽  
O. W. Holland
Keyword(s):  
Laser Power ◽  
Solid Phase ◽  
Solute Segregation ◽  
Dislocation Loops ◽  
Solid Phase Crystallization ◽  
Time Resolved ◽  
Plan View ◽  
Ion Channeling ◽  
Retrograde Solubility ◽  
Transmission Electron

ABSTRACTTime-resolved-reflectivity measurements have been combined with transmission electron microscopy (cross-section and plan-view), Rutherford backscattering and ion channeling techniques to study the details of laser induced solid phase epitaxial growth in In+ and Sb+ implanted silicon in the temperature range from 725 to 1500 °K. The details of microstructures including the formation of polycrystals, precipitates, and dislocations have been correlated with the dynamics of crystallization. There were limits to the dopant concentrations which could be incorporated into substitutional lattice sites; these concentrations exceeded retrograde solubility limits by factors up to 70 in the case of the Si-In system. The coarsening of dislocation loops and the formation of a/2<110>, 90° dislocations in the underlying dislocation-loop bands are described as a function of laser power.

Time-Resolved Reflectivity Study of Solid-Phase Epitaxial Regrowth in Relaxed and Strained Si1−xGex Epilayers

1992 ◽  
Vol 281 ◽  
Author(s):  
T. E. Haynes ◽  
C. Lee ◽  
K. S. Jones
Keyword(s):  
Composition Dependence ◽  
Solid Phase ◽  
Strain Relaxation ◽  
Alloy Layer ◽  
Atomic Fraction ◽  
Bulk Alloy ◽  
Strained Layers ◽  
Time Resolved ◽  
Epitaxial Regrowth ◽  
Different Types

ABSTRACTThe rate of solid-phase epitaxial regrowth has been studied using time-resolved reflectivity in three different types of SiGe/Si epilayers amorphized by ion implantation. In two of these cases, the alloy epilayer contained either 12% or 20% Ge, and the amorphization depth was greater than the thickness (2000 Å) of the SiGe alloy layer. Time-resolved reflectivity measurements showed that the rate of regrowth was not constant in these two cases, but first decreased after passing the SiGe/Si interface, and then increased. The minimum regrowth rate occurred closer to the SiGe/Si interface in the epilayers with the larger Ge atomic fraction. In the third type of sample, the alloy epilayer thickness was ∼7μm, so that the initial epilayer (15% Ge) had the lattice constant of the bulk alloy. Furthermore, amorphization and regrowth occurred entirely within the relaxed alloy layer. In this case, the regrowth rate was constant. The composition dependence of the regrowth-rate transient in the strained layers is discussed in the context of a ‘critical-thickness’ model of strain relaxation.

Sensitive, rapid procedure for time-resolved immunofluorometry of lutropin.

1988 ◽  
Vol 34 (8) ◽  
pp. 1640-1644 ◽  
Author(s):  
M J Khosravi ◽  
R C Morton ◽  
E P Diamandis
Keyword(s):  
Monoclonal Antibody ◽  
Solid Phase ◽  
Detection System ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Practical Procedure ◽  
Daily Monitoring ◽  
Fluorescence Measurements ◽  
Capture Antibody ◽  
Europium Chelate

Abstract In this new immunofluorometric method for quantification of lutropin in serum, the "sandwich" principle is combined with time-resolved fluorescence measurements, with the europium chelate 4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid (BCPDA) used as label. A monoclonal antibody to the alpha-subunit of lutropin is adsorbed onto the walls of white-opaque microtiter wells to form the solid-phase capture antibody, and a biotin-labeled soluble monoclonal antibody is used for antigen quantification. The detection system is completed with streptavidin, which has been linked to a protein bulking agent labeled with multiple BCPDA residues. In the presence of excess europium, the fluorescence of the final complex attached to captured lutropin molecules is measured on the dried solid phasse with an automated time-resolved fluorometer. The assay can be performed as a rapid (less than 60 min incubation) or regular (150 min incubation) procedure. The rapid assay is well-suited for routine daily monitoring of increasing or ovulatory lutropin concentrations; the regular assay, with its greater sensitivity (0.5 int. unit/L), is a practical procedure for lutropin measurements in hyposecretory states. The assay measures up to 240 int. units/L, and results compare well with those by a commercially available radioimmunoassay, an immunoradiometric assay, and another time-resolved immunofluorometric procedure.

Laser-excited immunofluorometric assay of prolactin, with use of antibodies coupled to lanthanide-labeled diethylenetriaminepentaacetic acid.

1986 ◽  
Vol 32 (7) ◽  
pp. 1323-1327 ◽  
Author(s):  
H Déchaud ◽  
R Bador ◽  
F Claustrat ◽  
C Desuzinges
Keyword(s):  
Plasma Sample ◽  
Solid Phase ◽  
Nitrogen Laser ◽  
Diethylenetriaminepentaacetic Acid ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Step Procedure ◽  
Polystyrene Tube ◽  
Sandwich Type ◽  
One Step

Abstract We describe an immunofluorometric assay for prolactin based on lanthanide labeling of a monoclonal antibody and measuring time-resolved fluorescence. In this "sandwich"-type assay, the label (Eu3+) was bound to the second antibody by means of a simple, rapid method involving the anhydride of diethylenetriaminepentaacetic acid. To measure the photoluminescence of europium (or other lanthanides), we have developed a time-resolved fluorometer with a nitrogen laser as the pulsed excitation source. During the assay, the solid-phase antibody immobilized inside a polystyrene tube is incubated with the plasma sample and the second antibody in a one-step procedure. Results for 67 human plasmas correlated well (r = 0.98) with those by an immunoradiometric method.

Assay of creatine kinase isoenzyme MB in serum with time-resolved immunofluorometry

1990 ◽  
Vol 36 (9) ◽  
pp. 1679-1683 ◽  
Author(s):  
E S Lianidou ◽  
T K Christopoulos ◽  
E P Diamandis
Keyword(s):  
Creatine Kinase ◽  
Laser Excitation ◽  
Solid Phase ◽  
Time Resolved ◽  
Creatine Kinase Isoenzyme ◽  
Phase Complex ◽  
Precision And Accuracy ◽  
Accuracy Indices ◽  
First Time ◽  
Creatine Kinase Isoenzyme Mb

Abstract We describe the first time-resolved immunofluorometric assay for creatine kinase (EC 2.7.3.2) isoenzyme MB (CK-MB) in serum. The assay is based on the formation of the complex: solid-phase anti-CK-MB-CK-MB-biotinylated anti-CK-BB-streptavidin-BCPDA-Eu3+, where anti-CK-MB and anti-CK-BB are monoclonal antibodies against the CK isoenzymes MB and BB, respectively, and BCPDA is the europium chelator 4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid. The solid-phase complex is fluorescent and is measured on the dry solid-phase (microtiter well) in a specially designed time-resolved fluorometer that uses laser excitation. The assay requires 25 microL of serum and is not affected by the presence of either CK-MM (up to 5000 micrograms/L) or CK-BB (up to 1000 micrograms/L) in the sample. Precision and accuracy indices for the assay were satisfactory.

scholarly journals Streptavidin-Polyvinylamine Conjugates Labeled with a Europium Chelate: Applications in Immunoassay, Immunohistochemistry, and Microarrays

2000 ◽  
Vol 46 (9) ◽  
pp. 1450-1455 ◽  
Author(s):  
Andreas Scorilas ◽  
Anders Bjartell ◽  
Hans Lilja ◽  
Christina Moller ◽  
Eleftherios P. Diamandis
Keyword(s):  
Solid Phase ◽  
Specific Antigen ◽  
Microarray Experiment ◽  
Immunohistochemical Localization ◽  
Macromolecular Complex ◽  
Serum Samples ◽  
Time Resolved ◽  
Europium Chelate ◽  
Highly Correlated ◽  
Detection Reagent

Abstract Background: The favorable properties of lanthanide chelates compared with conventional fluorescent probes have attracted considerable interest. A Eu3+ chelator, 4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid (BCPDA), has been synthesized previously. Methods: We here describe immunoassay, immunohistochemistry, and microarray applications of a new streptavidin-based universal polyvinylamine (PVA) detection reagent that is multiply labeled with the europium chelate of BCPDA. Solid-phase time-resolved immunofluorometric assays for biotinylated mouse IgG and prostate-specific antigen (PSA) were developed using the new conjugate as a detection reagent. The new conjugate was also used for the immunohistochemical localization of PSA expression in paraffin-embedded prostatic tissues. A model microarray with spotted biotinylated antibody as target was also performed. Results: Approximately 50–100 BCPDA moieties were covalently bound to PVA, which was then linked to streptavidin via biotin interaction. The macromolecular complex successfully recognized and bound biotinylated detection reagents, e.g., antibodies. The new reagent enabled measurement of solid phase-immobilized biotinylated mouse IgG with a detection limit of ∼1 pg/assay and demonstrated excellent linearity. In an ELISA-type sandwich PSA assay that included two PSA monoclonal antibodies using the new conjugate as detection reagent, we detected 0.001 μg/L PSA (∼100 fg or ∼3 amol/assay). Serum samples analyzed for PSA by this method and a commercial assay gave highly correlated results. The new reagent enabled excellent immunohistochemical localization of PSA expression in prostate tissues. Using the new reagent in a model microarray experiment with biotinylated mouse IgG as target, we demonstrated excellent spatial resolution of 5- to 10-nL microspots. Conclusions: The new detection reagent may find important applications in biotechnology.

Novel application of streptavidin-hapten derivatives as protein-tracer conjugate in competitive-type immunoassays involving biotinylated detection probes

1991 ◽  
Vol 37 (1) ◽  
pp. 58-63 ◽  
Author(s):  
M J Khosravi ◽  
R C Morton
Keyword(s):  
No Reduction ◽  
Solid Phase ◽  
Binding Activity ◽  
Fluorescence Signal ◽  
Antibody Immobilization ◽  
Aggregate Formation ◽  
Cross Link ◽  
Time Resolved ◽  
Biotin Binding ◽  
Detection Reagent

Abstract To investigate the use of streptavidin-hapten derivatives as potential protein-tracer conjugates for competitive-type immunoassays, we labeled streptavidin with cortisol and compared biotin-binding activity of the conjugates with that of unlabeled streptavidin. In this model system, streptavidin labeled with one to approximately 17 cortisol molecules retained its capability to cross-link a biotinylated protein on microtiter wells to a biotin-based general detection reagent developed for time-resolved fluorometry. Compared with unlabeled streptavidin, there was no reduction in the binding activity of the conjugate carrying as many as 2.6 cortisol molecules per molecule of streptavidin. Conjugation ratios greater than 4.4 showed a slight decrease in binding activity, presumably because of the aggregate formation evident at these labeling ratios. As expected, the conjugates were also capable of linking a solid-phase-bound anti-cortisol monoclonal antibody to the biotinylated detection reagent. The fluorescence signal generated increased almost linearly with increasing conjugation ratios from about three to nine cortisol molecules per molecule of streptavidin. At greater ratios, the assay response plateaued. The calibration curves obtained were typical for competitive-type immunoassays when the conjugates were incorporated in a cortisol assay based on a second-antibody immobilization approach.

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