The vapour pressures of saturated aqueous solutions of sodium chloride, sodium bromide, sodium nitrate, sodium nitrite, potassium iodate, and rubidium chloride at temperatures from 227 K to 323 K

1998 ◽  
Vol 30 (1) ◽  
pp. 59-71 ◽  
Author(s):  
Alexander Apelblat ◽  
Eli Korin
Keyword(s):  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Sodium Nitrite ◽  
Sodium Nitrate ◽  
Sodium Bromide ◽  
Potassium Iodate ◽  
Rubidium Chloride

scholarly journals Effect of Sodium Chloride, Sodium Nitrite and Sodium Nitrate on the Infectivity of Hepatitis E Virus

2020 ◽  
Vol 12 (4) ◽  
pp. 350-354 ◽  
Author(s):  
Alexander Wolff ◽  
Taras Günther ◽  
Thiemo Albert ◽  
Reimar Johne
Keyword(s):  
Sodium Chloride ◽  
Sodium Nitrite ◽  
Foodborne Pathogens ◽  
Sodium Nitrate ◽  
Hepatitis E Virus ◽  
Meat Products ◽  
Hepatitis E ◽  
High Salt ◽  
Genotype 3 ◽  
Raw Meat

Abstract Hepatitis E virus (HEV) infection can cause acute and chronic hepatitis in humans. The zoonotic HEV genotype 3, which is highly prevalent in Europe, is mainly transmitted by consumption of raw meat and raw meat products produced from infected pigs or wild boars. High salt concentrations represent an important measure to preserve meat products and to inactivate foodborne pathogens. Here, an HEV preparation in phosphate-buffered saline (PBS) was subjected to different salt concentrations and the remaining infectivity was measured in a cell culture assay. Treatments with up to 20% sodium chloride for 24 h at 23 °C, with and without addition of 0.015% sodium nitrite or 0.03% sodium nitrate, did not lead to virus inactivation as compared to PBS only. Conditions usually applied for short-term and long-term fermented raw sausages were simulated by incubation at 22 °C for up to 6 days and at 16 °C for up to 8 weeks, respectively. Only 2% sodium chloride with 0.015% sodium nitrite showed a weak (< 1 log10), but significant, infectivity reduction after 2 and 4 days as compared to PBS only. Addition of 2% sodium chloride and 0.03% sodium nitrate showed a slight, but not significant, decrease in infectivity after 2 and 8 weeks as compared to PBS only. In conclusion, HEV is highly stable at high salt concentrations and at salt conditions usually applied to preserve raw meat products.

Structures of additional crystal forms of Satellite tobacco mosaic virus grown from a variety of salts

2021 ◽  
Vol 77 (12) ◽  
Author(s):  
Alexander McPherson
Keyword(s):  
Sodium Chloride ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Particle ◽  
Ammonium Sulfate ◽  
Sodium Nitrate ◽  
Sodium Bromide ◽  
Crystal Forms ◽  
Amino Terminal ◽  
Satellite Tobacco Mosaic Virus

The structures of new crystal forms of Satellite tobacco mosaic virus (STMV) are described. These belong to space groups I2, P21212 (a low-resolution form), R3 (H3) and P23. The R3 crystals are 50%/50% twinned, as are two instances of the P23 crystals. The I2 and P21212 crystals were grown from ammonium sulfate solutions, as was one crystal in space group P23, while the R3 and the other P23 crystals were grown from sodium chloride, sodium bromide and sodium nitrate. The monoclinic and orthorhombic crystals have half a virus particle as the asymmetric unit, while the rhombohedral and cubic crystals have one third of a virus particle. RNA segments organized about the icosahedral twofold axes were present in crystals grown from ammonium sulfate and sodium chloride, as in the canonical I222 crystals (PDB entry 4oq8), but were not observed in crystals grown from sodium bromide and sodium nitrate. Bromide and nitrate ions generally replaced the RNA phosphates present in the I222 crystals, including the phosphates seen on fivefold axes, and were also found at threefold vertices in both the rhombohedral and cubic forms. An additional anion was also found on the fivefold axis 5 Å from the first anion, and slightly outside the capsid in crystals grown from sodium chloride, sodium bromide and sodium nitrate, suggesting that the path along the symmetry axis might be an ion channel. The electron densities for RNA strands at individual icosahedral dyads, as well as at the amino-terminal peptides of protein subunits, exhibited a diversity of orientations, in particular the residues at the ends.

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