Dielectric spectroscopy of solutions of amino silicone emulsion in distilled water

Author(s):  
K. N. Shah ◽  
V. A. Rana ◽  
C. M. Trivedi ◽  
H. P. Vankar
2021 ◽  
Vol 35 (11) ◽  
pp. 1404-1405
Author(s):  
Camilo Mendivelso ◽  
John Pantoja ◽  
Felix Vega ◽  
Chaouki Kasmi ◽  
Fahad Al Yafei

In this paper, the capability of sensing low concentrations of glyphosate in water of two interdigital capacitive transducers are analyzed using numerical simulations and measurements. Each microwave sensor is analyzed using the surface electric field produced at the resonance frequency. In addition, the reflection coefficient of each transducer submerged in water with glyphosate is measured and compared with distilled water. Prepared samples with concentrations of 1ppm/L (1 part per million over a liter of distilled water) are used for the experimental tests.


Author(s):  
Sydney S. Breese ◽  
Howard L. Bachrach

Continuing studies on the physical and chemical properties of foot-and-mouth disease virus (FMDV) have included electron microscopy of RNA strands released when highly purified virus (1) was dialyzed against demlneralized distilled water. The RNA strands were dried on formvar-carbon coated electron microscope screens pretreated with 0.1% bovine plasma albumin in distilled water. At this low salt concentration the RNA strands were extended and were stained with 1% phosphotungstic acid. Random dispersions of strands were recorded on electron micrographs, enlarged to 30,000 or 40,000 X and the lengths measured with a map-measuring wheel. Figure 1 is a typical micrograph and Fig. 2 shows the distributions of strand lengths for the three major types of FMDV (A119 of 6/9/72; C3-Rezende of 1/5/73; and O1-Brugge of 8/24/73.


Author(s):  
Russell L. Steere ◽  
Eric F. Erbe

It has been assumed by many involved in freeze-etch or freeze-fracture studies that it would be useless to etch specimens which were cryoprotected by more than 15% glycerol. We presumed that the amount of cryoprotective material exposed at the surface would serve as a contaminating layer and prevent the visualization of fine details. Recent unexpected freeze-etch results indicated that it would be useful to compare complementary replicas in which one-half of the frozen-fractured specimen would be shadowed and replicated immediately after fracturing whereas the complement would be etched at -98°C for 1 to 10 minutes before being shadowed and replicated.Standard complementary replica holders (Steere, 1973) with hinges removed were used for this study. Specimens consisting of unfixed virus-infected plant tissue infiltrated with 0.05 M phosphate buffer or distilled water were used without cryoprotectant. Some were permitted to settle through gradients to the desired concentrations of different cryoprotectants.


Author(s):  
Russell L. Steere ◽  
Eric F. Erbe

Thin sheets of acrylamide and agar gels of different concentrations were prepared and washed in distilled water, cut into pieces of appropriate size to fit into complementary freeze-etch specimen holders (1) and rapidly frozen. Freeze-etching was accomplished in a modified Denton DFE-2 freeze-etch unit on a DV-503 vacuum evaporator.* All samples were etched for 10 min. at -98°C then re-cooled to -150°C for deposition of Pt-C shadow- and C replica-films. Acrylamide gels were dissolved in Chlorox (5.251 sodium hypochlorite) containing 101 sodium hydroxide, whereas agar gels dissolved rapidly in the commonly used chromic acid cleaning solutions. Replicas were picked up on grids with thin Foimvar support films and stereo electron micrographs were obtained with a JEM-100 B electron microscope equipped with a 60° goniometer stage.Characteristic differences between gels of different concentrations (Figs. 1 and 2) were sufficiently pronounced to convince us that the structures observed are real and not the result of freezing artifacts.


Author(s):  
E. Keyhani

The matrix of biological membranes consists of a lipid bilayer into which proteins or protein aggregates are intercalated. Freeze-fracture techni- ques permit these proteins, perhaps in association with lipids, to be visualized in the hydrophobic regions of the membrane. Thus, numerous intramembrane particles (IMP) have been found on the fracture faces of membranes from a wide variety of cells (1-3). A recognized property of IMP is their tendency to form aggregates in response to changes in experi- mental conditions (4,5), perhaps as a result of translational diffusion through the viscous plane of the membrane. The purpose of this communica- tion is to describe the distribution and size of IMP in the plasma membrane of yeast (Candida utilis).Yeast cells (ATCC 8205) were grown in synthetic medium (6), and then harvested after 16 hours of culture, and washed twice in distilled water. Cell pellets were suspended in growth medium supplemented with 30% glycerol and incubated for 30 minutes at 0°C, centrifuged, and prepared for freeze-fracture, as described earlier (2,3).


Author(s):  
Eugene J. Amaral

Examination of sand grain surfaces from early Paleozoic sandstones by electron microscopy reveals a variety of secondary effects caused by rock-forming processes after final deposition of the sand. Detailed studies were conducted on both coarse (≥0.71mm) and fine (=0.25mm) fractions of St. Peter Sandstone, a widespread sand deposit underlying much of the U.S. Central Interior and used in the glass industry because of its remarkably high silica purity.The very friable sandstone was disaggregated and sieved to obtain the two size fractions, and then cleaned by boiling in HCl to remove any iron impurities and rinsed in distilled water. The sand grains were then partially embedded by sprinkling them onto a glass slide coated with a thin tacky layer of latex. Direct platinum shadowed carbon replicas were made of the exposed sand grain surfaces, and were separated by dissolution of the silica in HF acid.


Author(s):  
P. A. Madden ◽  
W. R. Anderson

The intestinal roundworm of swine is pinkish in color and about the diameter of a lead pencil. Adult worms, taken from parasitized swine, frequently were observed with macroscopic lesions on their cuticule. Those possessing such lesions were rinsed in distilled water, and cylindrical segments of the affected areas were removed. Some of the segments were fixed in buffered formalin before freeze-drying; others were freeze-dried immediately. Initially, specimens were quenched in liquid freon followed by immersion in liquid nitrogen. They were then placed in ampuoles in a freezer at −45C and sublimated by vacuum until dry. After the specimens appeared dry, the freezer was allowed to come to room temperature slowly while the vacuum was maintained. The dried specimens were attached to metal pegs with conductive silver paint and placed in a vacuum evaporator on a rotating tilting stage. They were then coated by evaporating an alloy of 20% palladium and 80% gold to a thickness of approximately 300 A°. The specimens were examined by secondary electron emmission in a scanning electron microscope.


Author(s):  
Russell L. Steere

Complementary replicas have revealed the fact that the two common faces observed in electron micrographs of freeze-fracture and freeze-etch specimens are complementary to each other and are thus the new faces of a split membrane rather than the original inner and outer surfaces (1, 2 and personal observations). The big question raised by published electron micrographs is why do we not see depressions in the complementary face opposite membrane-associated particles? Reports have appeared indicating that some depressions do appear but complementarity on such a fine scale has yet to be shown.Dog cardiac muscle was perfused with glutaraldehyde, washed in distilled water, then transferred to 30% glycerol (material furnished by Dr. Joaquim Sommer, Duke Univ., and VA Hospital, Durham, N.C.). Small strips were freeze-fractured in a Denton Vacuum DFE-2 Freeze-Etch Unit with complementary replica tooling. Replicas were cleaned in chromic acid cleaning solution, then washed in 4 changes of distilled water and mounted on opposite sides of the center wire of a Formvar-coated grid.


Author(s):  
H.A. Cohen ◽  
W. Chiu ◽  
J. Hosoda

GP 32 (molecular weight 35000) is a T4 bacteriophage protein that destabilizes the DNA helix. The fragment GP32*I (77% of the total weight), which destabilizes helices better than does the parent molecule, crystallizes as platelets thin enough for electron diffraction and electron imaging. In this paper we discuss the structure of this protein as revealed in images reconstructed from stained and unstained crystals.Crystals were prepared as previously described. Crystals for electron microscopy were pelleted from the buffer suspension, washed in distilled water, and resuspended in 1% glucose. Two lambda droplets were placed on grids over freshly evaporated carbon, allowed to sit for five minutes, and then were drained. Stained crystals were prepared the same way, except that prior to draining the droplet, two lambda of aqueous 1% uranyl acetate solution were applied for 20 seconds. Micrographs were produced using less than 2 e/Å2 for unstained crystals or less than 8 e/Å2 for stained crystals.


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