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- Aklint, T, et al.
(författare)
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Magnetic properties of deposited iron clusters produced in a high-yield laser vaporization source
- 1998
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Ingår i: APPLIED ORGANOMETALLIC CHEMISTRY. - : JOHN WILEY & SONS LTD. - 0268-2605. ; 12:7, s. 479-484
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Clusters of iron produced in a laser vaporization source have been characterized with time-of-flight spectra and deposited on different substrates for production of films of varying thickness. The magnetic properties of these films with thicknesses of 60
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- Cain, W.S., et al.
(författare)
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Comparison of models of Odor Interaction.
- 1995
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Ingår i: Chemical Senses. ; 20, s. 625-637
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Tidskriftsartikel (refereegranskat)abstract
- Subjects rated the overall perceived intensity of concentrations of the odorants cineole, geraniol, hexyl salicylate, and linalyl acetate smelled alone and in binary mixtures. The subjects also rated intensity of specified constituents (e.g. amount of cin
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- Lindgren, A, et al.
(författare)
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Paracetamol-induced cholestatic and granulomatous liver injuries.
- 1997
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Ingår i: Journal of internal medicine. - : Wiley. - 0954-6820 .- 1365-2796. ; 241:5, s. 435-9
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Tidskriftsartikel (refereegranskat)abstract
- To describe uncommon (previously unreported) types of adverse liver reactions to paracetamol.In addition to describing patients, with uncommon types of liver reactions to paracetamol, admitted to our hospitals, we surveyed all the liver reactions to paracetamol reported to the Swedish Adverse Drug Reactions Advisory Committee from 1973 to 1993.The Swedish population of 8 million inhabitants.Extensive medical evaluation.We found one case with a cholestatic liver reaction and one with granulomatous hepatitis. The reactions were probably idiosyncratic and took several months to disappear.In addition to the well-known dose-related toxic liver damage paracetamol may rarely cause non-dose-related severe, prolonged cholestasis or granulomatous hepatitis with cirrhosis.
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- Modig, C, et al.
(författare)
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Identification of betaIII- and betaIV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): antibody mapping and cDNA sequencing.
- 1999
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Ingår i: Cell motility and the cytoskeleton. - 0886-1544. ; 42:4, s. 315-30
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Tidskriftsartikel (refereegranskat)abstract
- Isolated microtubule proteins from the Atlantic cod (Gadus morhua) assemble at temperatures between 8 and 30 degrees C. The cold-adaptation is an intrinsic property of the tubulin molecules, but the reason for it is unknown. To increase our knowledge of tubulin diversity and its role in cold-adaptation we have further characterized cod tubulins using alpha- and beta-tubulin site-directed antibodies and antibodies towards posttranslationally modified tubulin. In addition, one cod brain beta-tubulin isotype has been sequenced. In mammals there are five beta-tubulins (betaI, betaII, betaIII, betaIVa and betaIVb) expressed in brain. A cod betaIII-tubulin was identified by its electrophoretic mobility after reduction and carboxymethylation. The betaIII-like tubulin accounted for more than 30% of total brain beta-tubulins, the highest yield yet observed in any animal. This tubulin corresponds most probably with an additional band, designated beta(x), which was found between alpha- and beta-tubulins on SDS-polyacrylamide gels. It was found to be phosphorylated and neurospecific, and constituted about 30% of total cod beta-tubulin isoforms. The sequenced cod tubulin was identified as a betaIV-tubulin, and a betaIV-isotype was stained by a C-terminal specific antibody. The amount of staining indicates that this isotype, as in mammals, only accounts for a minor part of the total brain beta-tubulin. Based on the estimated amounts of betaIII- and betaIV-tubulins in cod brain, our results indicate that cod has at least one additional beta-tubulin isotype and that beta-tubulin diversity evolved early during fish evolution. The sequenced cod betaIV-tubulin had four unique amino acid substitutions when compared to beta-tubulin sequences from other animals, while one substitution was in common with Antarctic rockcod beta-tubulin. Residues 221, Thr to Ser, and 283, Ala to Ser, correspond in the bovine tubulin dimer structure to loops that most probably interact with other tubulin molecules within the microtubule, and might contribute to cold-adaptation of microtubules.
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