Improvements in XRF specimen preparation using the dried residue method: Gallium in plutonium metal

2004 ◽  
Vol 19 (1) ◽  
pp. 87-89 ◽  
Author(s):  
Christopher G. Worley ◽  
Lisa P. Colletti
Keyword(s):  
Preparation Method ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specimen Preparation ◽  
Sample Analysis ◽  
Liquid Samples ◽  
Accuracy And Precision ◽  
Gallium Content ◽  
Method Accuracy ◽  
Plutonium Metal

Preparing dry specimens from liquid samples for XRF analysis avoids introducing caustic or hazardous liquids into the instrument. Several modifications were made to a dried residue specimen preparation method for quantifying gallium in plutonium metal in order to improve the method accuracy and precision. Ion exchange chromatography was utilized to remove the plutonium prior to casting the dried residue specimens. This, coupled with several other changes, improved the method relative error from ∼5% to less than 1%. These results are sufficient for routine sample analysis and are almost comparable to results from the established process using liquid specimens. However, the analysis of radioactive liquid specimens is unnecessary for quantifying the plutonium gallium content using this dried residue approach

scholarly journals Raman spectroscopic analysis of high molecular weight proteins in solution – considerations for sample analysis and data pre-processing

The Analyst ◽  
2018 ◽  
Vol 143 (24) ◽  
pp. 5987-5998 ◽  
Author(s):  
Drishya Rajan Parachalil ◽  
Brenda Brankin ◽  
Jennifer McIntyre ◽  
Hugh J. Byrne
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Multivariate Regression ◽  
Spectroscopic Analysis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Sample Analysis ◽  
Raman Spectroscopic ◽  
Regression Techniques ◽  
High Molecular Weight Proteins

This study explores the potential of Raman spectroscopy, coupled with multivariate regression techniques and ion exchange chromatography, to quantitatively monitor diagnostically relevant changes in high molecular weight proteins in liquid plasma.

Optimization of a dried residue specimen preparation method for quantifying analytes in plutonium metal using WDXRF

2007 ◽  
Vol 22 (2) ◽  
pp. 152-155 ◽  
Author(s):  
Christopher G. Worley ◽  
Lisa P. Colletti
Keyword(s):  
Thin Films ◽  
Preparation Method ◽  
Specimen Preparation ◽  
Preparation Time ◽  
Relative Precision ◽  
A Cell ◽  
Novel Method ◽  
Plutonium Metal

A novel method for preparing thin films was investigated for quantifying gallium and iron in plutonium solutions using WDXRF. This technique was developed to eliminate the potential for radioactive liquid to leak into the spectrometer, decrease specimen preparation time, and minimize waste. Samples were cast in μL quantities onto Kapton, and a surfactant was added to disperse the solution uniformly across the Kapton. After drying the specimens, they were sealed in a cell for analysis. Results to date indicate the method can provide a relative precision of ∼0.5% for gallium and ∼2% for iron, which is more than sufficient for routine sample analyses.

Comparison of microsublimation and ion exchange chromatography for boron isolation preceding its isotopic analysis via multi-collector ICP-MS

2014 ◽  
Vol 29 (10) ◽  
pp. 1819-1826 ◽  
Author(s):  
K. Van Hoecke ◽  
V. Devulder ◽  
P. Claeys ◽  
P. Degryse ◽  
F. Vanhaecke
Keyword(s):  
Ion Exchange ◽  
Removal Efficiency ◽  
Isotopic Analysis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Procedural Blank ◽  
Accuracy And Precision ◽  
Icp Ms ◽  
Isolation Methods ◽  
Matrix Removal

Two boron isolation methods, microsublimation and ion exchange chromatography, were compared in terms of B recovery, procedural blank, matrix removal efficiency, accuracy and precision of δ11B, labor intensiveness and costs.

Direct Observation of Heat Exchanger Deposits by Cross Sectioning

1967 ◽  
Vol 25 ◽  
pp. 364-365
Author(s):  
R. W. Anderson ◽  
D. L. Senecal
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Heat Exchanger ◽  
Direct Observation ◽  
Cross Sections ◽  
Preparation Method ◽  
Specimen Preparation ◽  
Flowing Water ◽  
Transmission Electron ◽  
Deposit Layer

A problem was presented to observe the packing densities of deposits of sub-micron corrosion product particles. The deposits were 5-100 mils thick and had formed on the inside surfaces of 3/8 inch diameter Zircaloy-2 heat exchanger tubes. The particles were iron oxides deposited from flowing water and consequently were only weakly bonded. Particular care was required during handling to preserve the original formations of the deposits. The specimen preparation method described below allowed direct observation of cross sections of the deposit layers by transmission electron microscopy.The specimens were short sections of the tubes (about 3 inches long) that were carefully cut from the systems. The insides of the tube sections were first coated with a thin layer of a fluid epoxy resin by dipping. This coating served to impregnate the deposit layer as well as to protect the layer if subsequent handling were required.

Scanning electron microscopy of human iliac bone by a simple preparation method

1990 ◽  
Vol 48 (3) ◽  
pp. 226-227
Author(s):  
Toshihiko Takita ◽  
Tomonori Naguro ◽  
Toshio Kameie ◽  
Akihiro Iino ◽  
Kichizo Yamamoto
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Preparation Method ◽  
Specimen Preparation ◽  
Real Surface ◽  
Public Attention ◽  
Preparation Methods ◽  
The Real ◽  
Simple Preparation ◽  
Scanning Electron

Recently with the increase in advanced age population, the osteoporosis becomes the object of public attention in the field of orthopedics. The surface topography of the bone by scanning electron microscopy (SEM) is one of the most useful means to study the bone metabolism, that is considered to make clear the mechanism of the osteoporosis. Until today many specimen preparation methods for SEM have been reported. They are roughly classified into two; the anorganic preparation and the simple preparation. The former is suitable for observing mineralization, but has the demerit that the real surface of the bone can not be observed and, moreover, the samples prepared by this method are extremely fragile especially in the case of osteoporosis. On the other hand, the latter has the merit that the real information of the bone surface can be obtained, though it is difficult to recognize the functional situation of the bone.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Preparation and Characterization of NH2-Terminal Fibrinogen Bβ Fragments from N-DSK of Human Fibrinogen

1984 ◽  
Vol 51 (01) ◽  
pp. 016-021 ◽  
Author(s):  
S Birken ◽  
G Agosto ◽  
B Lahiri ◽  
R Canfield
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Reverse Phase ◽  
Human Fibrinogen ◽  
Human Volunteers ◽  
Cnbr Cleavage ◽  
Two Peaks

SummaryIn order to investigate the early release of NH2-terminal plasmic fragments from the Bβ chain of fibrinogen, substantial quantities of Bβ 1-42 and Bβ 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and Bβ 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. Bβ 1-42 and Bβ 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of Bβ 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.

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