Polarographic studies with the dropping mercury kathode. Part XI. Overpotential of mercury deposited from mercuric salt solutions

1930 ◽  
Vol 2 ◽  
pp. 347-362 ◽  
Author(s):  
W. Kemula
Keyword(s):  
Salt Solutions ◽  
Mercuric Salt

Photoreduction of Mercuric Salt Solutions at High pH

1998 ◽  
Vol 32 (5) ◽  
pp. 670-675 ◽  
Author(s):  
Lisa D. Lau ◽  
RenÉ Rodriguez ◽  
Shannon Henery ◽  
David Manuel ◽  
Lynn Schwendiman
Keyword(s):  
Salt Solutions ◽  
High Ph ◽  
Mercuric Salt

Technical Note:Cracking of Aluminum Alloy 5083 in Mercuric Salt Solutions

CORROSION ◽  
1990 ◽  
Vol 46 (2) ◽  
pp. 159-161 ◽  
Author(s):  
J. J. Krupowicz ◽  
D. S. Hampton
Keyword(s):  
Aluminum Alloy ◽  
Salt Solutions ◽  
Aluminum Alloy 5083 ◽  
Mercuric Salt

Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

1983 ◽  
Vol 41 ◽  
pp. 446-447
Author(s):  
William F. Tivol ◽  
Murray Vernon King ◽  
D. F. Parsons
Keyword(s):  
Electron Diffraction ◽  
Heavy Atom ◽  
Isomorphous Substitution ◽  
X Ray Diffraction ◽  
Salt Solutions ◽  
X Ray ◽  
Isomorphous Replacement ◽  
Structure Factors ◽  
Diffraction Structure ◽  
The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

Bulk standards for low-temperature biological x-ray microanalysis

1984 ◽  
Vol 42 ◽  
pp. 282-283
Author(s):  
P. Echlin ◽  
M. McKoon ◽  
E.S. Taylor ◽  
C.E. Thomas ◽  
K.L. Maloney ◽  
...  
Keyword(s):  
Phase Separation ◽  
Low Temperature ◽  
Analytical Method ◽  
Salt Solutions ◽  
Absolute Concentration ◽  
Cooling Process ◽  
X Ray ◽  
The Absolute ◽  
Analytical Procedures ◽  
Electrical Conductors

Although sections of frozen salt solutions have been used as standards for x-ray microanalysis, such solutions are less useful when analysed in the bulk form. They are poor thermal and electrical conductors and severe phase separation occurs during the cooling process. Following a suggestion by Whitecross et al we have made up a series of salt solutions containing a small amount of graphite to improve the sample conductivity. In addition, we have incorporated a polymer to ensure the formation of microcrystalline ice and a consequent homogenity of salt dispersion within the frozen matrix. The mixtures have been used to standardize the analytical procedures applied to frozen hydrated bulk specimens based on the peak/background analytical method and to measure the absolute concentration of elements in developing roots.

Solution behavior of quenched or strongly charged polyampholytes in aqueous-salt solutions

2019 ◽  
Vol 94 (2) ◽  
pp. 35-44 ◽  
Author(s):  
G. Toleutay ◽  
◽  
A.V. Shakhvorostov ◽  
S.K. Kabdrakhmanova ◽  
S.E. Kudaibergenov ◽  
...  
Keyword(s):  
Salt Solutions ◽  
Solution Behavior ◽  
Aqueous Salt Solutions
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