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- Sargeson, A. M., et al.
(author)
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Names and symbols for the transfermium elements
- 1997
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In: Pure and Applied Chemistry. - : Walter de Gruyter GmbH. - 0033-4545 .- 1365-3075. ; 69:12, s. 2471-2473
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Journal article (peer-reviewed)abstract
- The recommendations (ref. 1) of the Commission on Nomenclature of Inorganic Chemistry (CNIC) on the nomenclature of the transfermium elements (101-109, inclusive) were considered by the IUPAC Bureau at Guildford (UK) in September 1995. As a result of the various criticisms of the recommendations and theway that they had been processed, the Bureau decided to adopt the recommendations as provisional and to circulate them to national/regional nomenclature centres in the normal way, with notices to be published innational/regional chemistry journals and magazines, requesting submission of comments to CNIC. In particular, the National Adhering Organizations (NAOs) were invited to express their views concerning the extant proposals for the names of these elements and the principles and traditions used to derive them. The response from the general chemical community was small, and the bulk of the replies came from nuclear scientists.
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- Garcia-Guzman, M, et al.
(author)
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Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue.
- 1997
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In: Molecular Pharmacology. - 0026-895X .- 1521-0111. ; 51:1, s. 109-18
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Journal article (peer-reviewed)abstract
- We isolated a cDNA from human brain encoding a purinergic receptor that shows a high degree of homology to the rat P2X4 receptor (87% identity). By fluorescence in situ hybridization, the human P2X4 gene has been mapped to region q24.32 of chromosome 12. Tissue distribution analysis of human P2X4 transcripts demonstrates a broad expression pattern in that the mRNA was detected not only in brain but also in all tissues tested. Heterologous expression of the human P2X4 receptor in Xenopus laevis oocytes and human embryonic kidney 293 cells evoked an ATP-activated channel. Simultaneous whole-cell current and Fura-2 fluorescence measurements in human embronic kidney 293 cells transfected with human P2X4 cDNA allowed us to determine the fraction of the current carried by Ca2: this was approximately 8%, demonstrating a high Ca2+ permeability. Low extracellular Zn2+ concentrations (5-10 microM) increase the apparent gating efficiency of human P2X4 by ATP without affecting the maximal response. However, raising the concentration of the divalent cation (> 100 microM) inhibits the ATP-evoked current in a non-voltage-dependent manner. The human P2X4 receptor displays a very similar agonist potency profile to that of rat P2X4 (ATP > > 2-methylthio-ATP > or = CTP > alpha, beta-methylene-ATP > dATP) but has a notably higher sensitivity for the antagonists suramin, pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid, and bromphenol blue. Chimeric constructs between human and rat isoforms as well as single-point mutations were engineered to map the regions responsible for the different sensitivity to suramin and pyridoxal-phosphate-6-azophenyl-2'4'-disulfonic acid.
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- Khayyami, M, et al.
(author)
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Development of an amperometric biosensor based on acetylcholine esterase covalently bound to a new support material
- 1998
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In: Talanta. - 1873-3573. ; 45:3, s. 557-563
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Journal article (peer-reviewed)abstract
- A new type of amperometric biosensor based on immobilised acetylcholine esterase was designed and constructed. The enzyme was immobilised on a flow-through working electrode, which was prepared from reticulated vitreous carbon (RVC) or from a composite material consisting of RVC and superporous agarose. The sensor was operated in FIA mode using acetylthiocholine as a substrate. The sensor responded to inhibitors such as paraoxon—10−9 mol was detected by the sensor in a non-optimised configuration. The practical lifetime of the sensor was at least 1 month.
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