Quality assurance: Evaluation and comparison of methods for electron microscopic measurement of GBM width and the effect of in‐lab calibration in diagnostic renal pathology

2021 ◽  
Author(s):  
Meral Uner ◽  
Secil Demirkol Canlı ◽  
Lois J. Arend
Keyword(s):  
Quality Assurance ◽  
Renal Pathology ◽  
Comparison Of Methods ◽  
Electron Microscopic ◽  
Microscopic Measurement

scholarly journals Anti-Corrosion Behavior of Olmesartan for Soft-Cast Steel in 1 mol dm−3 HCl

Coatings ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 965
Author(s):  
B. M. Praveen ◽  
A. Alhadhrami ◽  
B. M. Prasanna ◽  
Narayana Hebbar ◽  
Radhakrishna Prabhu
Keyword(s):  
Inhibition Efficiency ◽  
Elevated Temperatures ◽  
Cast Steel ◽  
Protective Layer ◽  
Electron Microscopic ◽  
Higher Temperature ◽  
Steel Surfaces ◽  
Dynamics Simulations ◽  
Microscopic Measurement ◽  
Inhibitive Action

This study discusses the effects of temperature on corrosion inhibition for soft-cast steel by the pharmaceutically active drug olmesartan in 1 mol dm−3 HCl. The sufficient number of electron-rich elements and non-bonding π electrons in its structure favored a good capability for coating onto the electron-deficient steel surfaces. Theoretical and electrochemical measurements were carried out at the temperature region of 303 K to 333 K. Therefore, the experiment suggests that the inhibition efficiency of olmesartan increases with its increasing concentrations due to the adsorption. Additionally, even at a higher temperature of 333 K, the inhibitor molecules attain their stability towards corrosion resistance of steel surfaces. The adsorption of inhibitors on steel surfaces is spontaneously found to include the mixture of physisorption and chemisorption, and it obeys Temkin’s adsorption isotherm model. Theoretical and computational considerations were made using quantum chemical parameters and molecular dynamics simulations, which confirmed that the olmesartan has a suitable corrosion inhibitive capability intended for soft-cast steel in 1 mol dm−3 HCl. Additionally, scanning electron microscopic measurement was used to obtain a visual idea of the inhibitive action of the inhibitor attained by forming an adsorbed protective layer onto the steel surfaces. The minute concentration of olmesartan of about 10–50 ppm shows high inhibition efficiency of ~80%, even at elevated temperatures.

scholarly journals Electron microscopic measurement of chain flexibility of poly(dG-dC.poly(dG-dC) modified by cis-diamminedichloroplatinum(II)

1984 ◽  
Vol 12 (22) ◽  
pp. 8349-8362 ◽  
Author(s):  
B. Revet ◽  
J.M. Malinge ◽  
E. Delain ◽  
M.Le Bret ◽  
M. Leng
Keyword(s):  
Electron Microscopic ◽  
Chain Flexibility ◽  
Microscopic Measurement

scholarly journals Electron Microscopic Measurement of the Size of the Optical Focus in Laser Scanning Microscopy

2012 ◽  
Vol 18 (3) ◽  
pp. 596-602 ◽  
Author(s):  
Alison McDonald ◽  
William B. Amos ◽  
Gail McConnell
Keyword(s):  
Laser Scanning ◽  
Spot Size ◽  
Aluminum Film ◽  
Laser Scanning Microscopy ◽  
Electron Microscopic ◽  
Focal Spot Size ◽  
Glass Coverslip ◽  
Infrared Wavelengths ◽  
Microscopic Measurement ◽  
20 Nm

AbstractWe describe a method for measuring the lateral focal spot size of a multiphoton laser scanning microscope (LSM) with unprecedented accuracy. A specimen consisting of an aluminum film deposited on a glass coverslip was brought into focus in a LSM and the laser intensity was then increased enough to perform nanoablation of the metal film. This process leaves a permanent trace of the raster path usually taken by the beam during the acquisition of an optical image. A scanning electron microscope (SEM) was then used to determine the nanoablated line width to high accuracy, from which the lateral spot size and hence resolution of the LSM can be determined. To demonstrate our method, we performed analysis of a multiphoton LSM at various infrared wavelengths, and we report measurements of optical lateral spot size with an accuracy of 20 nm, limited only by the resolution of the SEM.

A Reproducible Selective Stain for Cardiac Sarcoplasmic Reticulum

1974 ◽  
Vol 32 ◽  
pp. 214-215
Author(s):  
R. A. Waugh ◽  
J. R. Sommer
Keyword(s):  
Complex System ◽  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Transmission Electron Microscope ◽  
Electron Microscopic ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Transmission Electron

Cardiac sarcoplasmic reticulum (SR) is a complex system of intracellular tubules that, due to their small size and juxtaposition to such electron-dense structures as mitochondria and myofibrils, are often inconspicuous in conventionally prepared electron microscopic material. This study reports a method with which the SR is selectively “stained” which facilitates visualizationwith the transmission electron microscope.

Electron Microscopic Study of the Epithelium of the Seminal Vesicle of Aging Rats

1974 ◽  
Vol 32 ◽  
pp. 138-139
Author(s):  
V. F. Allison ◽  
G. C. Fink ◽  
G. W. Cearley
Keyword(s):  
Cell Growth ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Seminal Vesicles ◽  
Epithelial Layer ◽  
Epithelial Hyperplasia ◽  
Electron Microscopic ◽  
Aging Rats ◽  
Pseudostratified Epithelium

It is well known that epithelial hyperplasia (benign hypertrophy) is common in the aging prostate of dogs and man. In contrast, little evidence is available for abnormal epithelial cell growth in seminal vesicles of aging animals. Recently, enlarged seminal vesicles were reported in senescent mice, however, that enlargement resulted from increased storage of secretion in the lumen and occurred concomitant to epithelial hypoplasia in that species.The present study is concerned with electron microscopic observations of changes occurring in the pseudostratified epithelium of the seminal vescles of aging rats. Special attention is given to certain non-epithelial cells which have entered the epithelial layer.

The Growth of Herpesvirus mulatto in Human Fibroblast

1974 ◽  
Vol 32 ◽  
pp. 244-245
Author(s):  
Glennelle Washington ◽  
Philip P. McGrath ◽  
Peter R. Graze ◽  
Ivor Royston
Keyword(s):  
Rhesus Monkey ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Peripheral Blood ◽  
Human Fibroblast ◽  
Rhesus Monkeys ◽  
Human Fibroblasts ◽  
Electron Microscopic ◽  
Specific Antisera ◽  
Peripheral Blood Leucocytes

Herpes-like viruses were isolated from rhesus monkey peripheral blood leucocytes when co-cultivated with WI-38 cells. The virus was originally designated rhesus leucocyte-associated herpesvirus (LAHV) and subsequently called Herpesvirus mulatta (HVM). The original isolations were from juvenile rhesus monkeys shown to be free of antibody to rhesus cytomegalic virus. The virus could only be propagated in human or simian fibroblasts. Use of specific antisera developed from HVM showed no relationship between this virus and other herpesviruses. An electron microscopic study was undertaken to determine the morphology of Herpesvirus mulatta (HVM) in infected human fibroblasts.

Observation of biological macromolecules using various electron microscopic methods

1978 ◽  
Vol 36 (2) ◽  
pp. 170-171
Author(s):  
Mitsuo Ohtsuki ◽  
Michael Sogard
Keyword(s):  
Electron Microscope ◽  
Phase Contrast ◽  
Image Interpretation ◽  
Density Lipoprotein ◽  
Biological Macromolecules ◽  
Contrast Effects ◽  
Biological Structure ◽  
Electron Microscopic ◽  
Structural Investigations ◽  
Staining Techniques

Structural investigations of biological macromolecules commonly employ CTEM with negative staining techniques. Difficulties in valid image interpretation arise, however, due to problems such as variability in thickness and degree of penetration of the staining agent, noise from the supporting film, and artifacts from defocus phase contrast effects. In order to determine the effects of these variables on biological structure, as seen by the electron microscope, negative stained macromolecules of high density lipoprotein-3 (HDL3) from human serum were analyzed with both CTEM and STEM, and results were then compared with CTEM micrographs of freeze-etched HDL3. In addition, we altered the structure of this molecule by digesting away its phospholipid component with phospholipase A2 and look for consistent changes in structure.

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