PubMed · 8917850
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N K Veien. 1996. Routine patch testing with AlCl3.. https://doi.org/10.1111/j.1600-0536.1996.tb02321.x
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A novel strategy, based on the addition of a cationic surfactant, for preventing the interferences associated with a diminution in the efficacy of solid-phase extraction (SPE) with silica cartridges of diquat, paraquat and difenzoquat in water is developed. Conditions for extraction are optimised with respect to pH, cationic surfactant and its concentration. Humic acids, anionic surfactants, inorganic salts and other organic contaminants like pesticides, phenols, polycyclic aromatic hydrocarbons and polychlorinated biphenyls produce the studied interferences. The best performance is shown in the improvement of the "quats" recovery from waters with high levels of humic acids and anionic surfactants (recovery is increased from ca. 30% to more than 80%). Unfortunately, the strong interference from inorganic salts remains. The presence in the water sample of other organic contaminants only affected the extraction efficiency of difenzoquat at high concentrations (more than 1 mg/l). Analytic utility is illustrated by selective measurements of the three herbicides, in real water samples. Overall, the results show that in spite of its drawbacks, SPE is a useful technique that allows the detection and quantification of the "quats" at limits below 100 ng/l as established by the European Union.
RGS proteins (regulators of G protein signaling) are GTPase activating proteins (GAPs) for Gi and Gq families of heterotrimeric G proteins but have not been found to interact with Gs alpha. The Gs alpha residue Asp229 has been suggested to be responsible for the inability of RGS proteins to interact with Gs alpha [Natochin, M., and Artemyev, N. O. (1998) J. Biol. Chem. 273, 4300-4303]. To test this hypothesis, we have investigated the possibility of generating an interaction between Gs alpha and RGS proteins by substituting Gs alpha Asp229 with Ser and replacing the potential Gs alpha Asp229 contact residues in RGS16, Glu129 and Asn131, by Ala and Ser, respectively. RGS16 and its mutants failed to interact with Gs alpha. A single mutation of Gs alpha, Asp229Ser, rendered the Gs alpha subunit with the ability to interact with RGS16 and RGS4. Like RGS protein binding to Gi and Gq alpha-subunits, RGS16 preferentially recognized the AlF4--bound conformation of Gs alpha Asp229Ser. In a single-turnover assay, RGS16 maximally stimulated GTPase activity of Gs alpha Asp229Ser by approximately 5-fold with an EC50 value of 7.5 microM. Our findings demonstrate that Asp229 of Gs alpha represents a major barrier for Gs alpha interaction with known RGS proteins.
Male rats were treated daily with an intraperitoneal injection of 15 mg aluminum (Al chloride)/kg body weight for 17 d, in order to study the effects on superoxide dismutase (SOD) activities in the brain (cortex). No significant difference between control and treated animals was registered in the Cu/Zn and Mn SOD activities in the gray matter of the cortex. High Al levels were found in the plasma, the spleen, and the liver of the treated animals in comparison to the controls, but not in the cortex homogenates (gray matter). In addition, Al induced a significant decrease in food ingestion and weight gain.