An improved method to estimate ultrasonic absorption in agar-based gel phantom using thermocouples and MR thermometry

Ultrasonics ◽  
2020 ◽  
Vol 103 ◽  
pp. 106089 ◽  
Author(s):  
T. Drakos ◽  
M. Giannakou ◽  
G. Menikou ◽  
C. Ioannides ◽  
C. Damianou
Keyword(s):  
Ultrasonic Absorption ◽  
Improved Method ◽  
Mr Thermometry ◽  
Gel Phantom

An Improved Method for the Preparation and TEM Examination of Sharp Pointed Tips used in APFIM and STM

1990 ◽  
Vol 48 (2) ◽  
pp. 102-103
Author(s):  
E.A. Fischione ◽  
P.E. Fischione ◽  
J.J. Haugh ◽  
M.G. Burke
Keyword(s):  
Atom Probe ◽  
Preparation Process ◽  
Improved Method ◽  
Ion Milling ◽  
Polishing Process ◽  
Probe Field ◽  
Scanning Tunnelling ◽  
Stm Tips ◽  
Tunnelling Microscopy ◽  
Ion Microscopy

A common requirement for both Atom Probe Field-Ion Microscopy (APFIM) and Scanning Tunnelling Microscopy (STM) is a sharp pointed tip for use as either the specimen (APFIM) or the probe (STM). Traditionally, tips have been prepared by either chemical or electropolishing techniques. Recently, ion-milling has been successfully employed in the production of APFIM tips [1]. Conventional electropolishing techniques are applicable to a wide variety of metals, but generally require careful manual adjustments during the polishing process and may also be time-consuming. In order to reduce the time and effort involved in the preparation process, a compact, self-contained polishing unit has been developed. This system is based upon the conventional two-stage electropolishing technique in which the specimen/tip blank is first locally thinned or “necked”, and subsequently electropolished until separation occurs.[2,3] The result of this process is the production of two APFIM or STM tips. A mechanized polishing unit that provides these functions while automatically maintaining alignment has been designed and developed.

Immunoelectron microscopic localization of elastic tissue in archival material using an improved method

1990 ◽  
Vol 48 (3) ◽  
pp. 794-795
Author(s):  
J. C. Fanning ◽  
J. F. White ◽  
R. Polewski ◽  
E. G. Cleary
Keyword(s):  
Normal Animal ◽  
Animal Tissue ◽  
Elastic Tissue ◽  
Human Tissues ◽  
Improved Method ◽  
Tissue Samples ◽  
Archival Material ◽  
Immuno Electron Microscopy ◽  
Arteries And Veins ◽  
Biochemical Examination

Elastic tissue is an important component of the walls of arteries and veins, of skin, of the lungs and in lesser amounts, of many other tissues. It is responsible for the rubber-like properties of the arteries and for the normal texture of young skin. It undergoes changes in a number of important diseases such as atherosclerosis and emphysema and on exposure of skin to sunlight.We have recently described methods for the localizationof elastic tissue components in normal animal and human tissues. In the study of developing and diseased tissues it is often not possible to obtain samples which have been optimally prepared for immuno-electron microscopy. Sometimes there is also a need to examine retrospectively samples collected some years previously. We have therefore developed modifications to our published methods to allow examination of human and animal tissue samples obtained at surgery or during post mortem which have subsequently been: 1. stored frozen at -35° or -70°C for biochemical examination; 2.

Intensifying Negatives–Improved Method

1895 ◽  
Vol 39 (1003supp) ◽  
pp. 16026-16027
Author(s):  
John Vansant
Keyword(s):  
Improved Method

SERUM TRIIODOTHYRONINE DETERMINATION BY SATURATION ANALYSIS

1973 ◽  
Vol 72 (4) ◽  
pp. 714-726 ◽  
Author(s):  
A. Burger ◽  
B. Miller ◽  
C. Sakoloff ◽  
M. B. Vallotton
Keyword(s):  
Ionic Strength ◽  
Limit Of Detection ◽  
Improved Method ◽  
Accuracy Of Measurement ◽  
Tracer Amount ◽  
The Mean ◽  
Physiological Values ◽  
Hyperthyroid Patients ◽  
Solvent Blank

ABSTRACT An improved method for the determination of serum triiodothyronine (T3) has been developed. After addition of a tracer amount of the hormone, T3 was extracted from 1 ml serum under conditions of pH and ionic strength which favoured T3 extraction (89%) over thyroxine (T4) extraction (58%). Chromatography of the extracted material on Sephadex LH-20 separated T3 completely from residual T4. The T3 eluate was dried, then re-dissolved in 0.5 ml NaOH 0.04 n. To 0.2 ml duplicate aliquots, a standard amount of TBG was added for the competitive protein analysis. After one hour incubation at 4°C, separation of bound from free T3 was achieved on small Sephadex G-25 columns. Overall recovery was 67 ± 10.8% and correction for the loss was made. The solvent blank was 37 ± 27 (sd) ng/100 ml. Accuracy of measurement of known quantities of T3 added to serum was 98.4%. The coefficient of variation within the assay was 6.2% and between the assays it was 11.4%. The limit of detection (0.1 ng) corresponded to a concentration of 25 ng/100 ml. T4 added to serum did not interfere with T3 determination until high non-physiological values were reached. The mean ± sd serum T3 in 54 euthyroid subjects was 153 ± 58 ng/100 ml and in 24 hyperthyroid patients it was 428 ±186 ng/100 ml; 4 out of the 24 hyperthyroid values were within 2 sd of the mean euthyroid group. All the values found in the euthyroid group were well above the limit of detection of the method.

AN IMPROVED METHOD FOR THE ASSAY OF PROGESTERONE BY COMPETITIVE PROTEIN BINDING

1970 ◽  
Vol 63 (2) ◽  
pp. 225-241 ◽  
Author(s):  
B. D. Reeves ◽  
M. L. A. de Souza ◽  
I. E. Thompson ◽  
E. Diczfalusy
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Entire Range ◽  
Improved Method ◽  
Plasma Progesterone ◽  
Extraction And Purification ◽  
Corticosteroid Binding Globulin ◽  
Competitive Protein Binding ◽  
The Individual ◽  
Range Of Values

ABSTRACT An improved method for the assay of plasma progesterone by competitive protein binding is described. The improvement is based upon rigorous control of the variables, the compensation for and standardisation of interfering factors inherent in the method and the use of a human corticosteroid binding globulin, that meets the requirements for sensitivity at levels of 1.0 ng of progesterone and below. The assessment of the reliability of the individual steps in the method as well as that of the complete method is presented. The sensitivity of the method is around 0.2 ng progesterone per ml plasma. Accuracy was measured by adding progesterone in amounts ranging from 0.0 to 1.0 ng to 1.0 ml plasma. There was a linear relationship between the progesterone added and recovered throughout the entire range of values, with a coefficient of correlation (r) of 0.94. Of 52 related steroids tested, none was found which would remain associated with progesterone following extraction and purification and which would also compete with progesterone for binding sites.

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