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Sökning: L773:0028 0836 OR L773:1476 4687 > (1980-1989)

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  • Ahlberg, Per E. (författare)
  • Fossil fishes from Gogo
  • 1989
  • Ingår i: Nature. - 0028-0836 .- 1476-4687. ; 337, s. 511-512
  • Tidskriftsartikel (övrigt vetenskapligt)
  • Baekkeskov, Steinunn, et al. (författare)
  • Autoantibodies in newly diagnosed diabetic children immunoprecipitate human pancreatic islet cell proteins
  • 1982
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 298:5870, s. 167-169
  • Tidskriftsartikel (refereegranskat)abstract
    • Insulin-dependent diabetic (IDD) patients have a high prevalence of circulating autoantibodies against islet of Langerhans cells at the time of diagnosis1-4. Inflammatory cells within the islets5, leukocyte migration inhibition in response to pancreatic antigens6 and an association with certain HLA-D/DR histocompatibility antigens 7,8, have also been observed. It seems that the autoantibodies may be pathogenically relevant as they react primarily with β-cells9, but the specific target antigen(s) have yet to be identified. In the present study we determined whether sera from insulin-dependent diabetic children are able to immunoprecipitate proteins from detergent lysates of human islet cells. We report that sera from 8 out of 10 newly diagnosed diabetic children consistently immunoprecipitate a protein having a molecular weight (M r) of ∼64,000 (64K). An additional protein (38K) was precipitated from islet cells obtained from a HLA-DR3-positive donor. Neither of the proteins was precipitated by non-diabetic sera nor detected in immunoprecipitates from human lymphocyte lysates. It is suggested that the 64K and/or 38K protein components may represent cell-specific target antigens in insulin-dependent diabetes.
  • Björck, Lars, et al. (författare)
  • Bacterial growth inhibited by a synthetic inhibitor based upon the structure of a human proteinase inhibitor
  • 1989
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 337:6205, s. 385-386
  • Tidskriftsartikel (refereegranskat)abstract
    • Cysteine proteinases are important not only in the intracellular catabolism of peptides and proteins1 and in the processing of prohormones and proenzymes2,3, but also in the penetration of normal human tissue by malignant cells4 and possibly microorganisms5, including viruses. Cystatin C is a human cysteine proteinase inhibitor present in extracellular fluids6. We have synthesized peptide derivatives mimicking the proposed proteinase-binding centre of cystatin C7 and find that they irreversibly inhibit cysteine proteinases. Several bacteria produce proteinases, so we tested a tripeptide derivative (Z-LVG-CHN2) for in vitro anti-bacterial activity against a large number of bacterial strains belonging to thirteen different species. It was found to inhibit specifically the growth of all strains of group A streptococci. The susceptibility of these human pathogens to the peptide was compared with that to well-established anti-streptococcal antibiotics such as tetracy-cline and bacitracin. Moreover, the peptide was active in vivo against group A streptococci: mice injected with lethal doses of these bacteria were cured by a single injection of Z-LVG-CHN2. The cysteine proteinase produced by group A streptococci was isolated and found to be inhibited by Z-LVG-CHN2; moreover, excess proteinase relieved the growth inhibition caused by the peptide derivative, suggesting that the antibacterial activity of Z-LVG-CHN2 is due to inhibition of this cysteine proteinase. This strategy of blocking proteinases with peptide derivatives that mimic naturally occurring inhibitors could be useful in the construction of new agents against other microorganisms, including viruses.
  • Böhme, Jan, et al. (författare)
  • Human class II major histocompatibility antigen β-chains are derived from at least three loci
  • 1983
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 301:5895, s. 82-84
  • Tidskriftsartikel (refereegranskat)abstract
    • Class II antigens of the major histocompatibility complex (MHC) consist of two glycosylated, membrane-integrated polypeptide chains1. These cell surface-expressed molecules are involved in several immunobiological events involving cell-cell interactions2,3, most of which seem to require that genetically identical class II antigens, or other molecules controlled by the same region of the MHC, are expressed on the interacting cells4. The extensive genetic polymorphism of the class II antigens5 has rendered analyses in the human system of the number of non-allelic species of class II antigens difficult, although several laboratories have reported the existence of at least two types of human class II antigens6-9. Here we present the results of experiments using restriction enzyme digestions and separation of DNA from individuals homozygous for the MHC followed by hybridization to human class II antigen α-10,11 and β-12-14 chain cDNA probes. While the α -chain probe gave only a single hybridization band, the various β -chain probes revealed a more complex pattern that is consistent with the existence of at least three separate β -chain genes or pseudogenes in the human MHC.
  • Hansen, Staffan, et al. (författare)
  • Oxidation Catalysis on YBa2Cu3O6 + x
  • 1988
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 334:6178, s. 143-145
  • Tidskriftsartikel (refereegranskat)abstract
    • Mild oxidation catalysts are used to product a wide range industrial chemicals from hydrocarbons, whereas deep oxidation catalysts yield CO2 and are becoming important in the cleaning of emissions from combustion of carbonaceous fuels. Here we report on a catalyst1 that facilitates both mild and deep oxidation of toluene in the presence of molecular oxygen and ammonia. At low partial pressures of O2a YBa2Cu3O6+x catalyst is very active in the formation of benzonitrile, but at higher O2 partial pressures it preferentially catalyses formation of CO2. This sharp transition in product selectivity is reversible and occurs at a defined partial pressure of O2. At transition the bulk compostition of the catalyst is close to YBa2Cu3O6 (x≈0). Increasing the content of lattice oxygen (x > 0) makes the catalyst selective for CO2 formation
  • Kilchherr, François, et al. (författare)
  • Isolation of the paired gene of Drosophila and its spatial expression during early embryogenesis
  • 1986
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 321:6069, s. 493-499
  • Tidskriftsartikel (refereegranskat)abstract
    • We have cloned the paired gene of Drosophila melanogaster, a pair-rule gene required for the establishment of proper segmentation. The transcriptional pattern in young embryos shows developmental polarities along the antero-posterior and dorso-ventral axes. Transcripts, initially expressed with a double-segment periodicity, switch to a single-segment repeat during syncytial blastoderm.
  • Moore, R.L., et al. (författare)
  • Superluminal Acceleration in 3C345
  • 1983
  • Ingår i: Nature. - London, United Kingdom : Nature Publishing Group. - 0028-0836. ; 306:5938, s. 44-46
  • Tidskriftsartikel (refereegranskat)abstract
    • The superluminal quasar 3C345 has a curved, one-sided jet-like radio structure1,2. Ejected material has been observed travelling at apparent speeds of 13–17c (ref. 3). We report here new observations at 22 GHz which show that the most recently ejected component4 is not moving radially away from the compact radio core, but along a trajectory which could be interpreted as either a curved path originating in the compact core, or a straight line, in which case the origin of ejection is not coincident with the compact radio core. The observations provide evidence of acceleration of this component. © 1983 Nature Publishing Group.
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