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- Choularton, T. W., et al.
(författare)
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The Great Dun Fell Cloud Experiment 1993 : An overview
- 1997
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Ingår i: Atmospheric Environment. - 1352-2310. ; 31:16, s. 2393-2405
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Tidskriftsartikel (refereegranskat)abstract
- The 1993 Ground-based Cloud Experiment on Great Dun Fell used a wide range of measurements of trace gases, aerosol particles and cloud droplets at five sites to study their sources and sinks especially those in cloud. These measurements have been interpreted using a variety of models. The conclusions add to our knowledge of air pollution, acidification of the atmosphere and the ground, eutrophication and climate change. The experiment is designed to use the hill cap cloud as a flow-through reactor, and was conducted in varying levels of pollution typical of much of the rural temperate continental northern hemisphere in spring-time.
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- Boström, Barbro, et al.
(författare)
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Survey of post-operative patients' pain management
- 1997
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Ingår i: Journal of Nursing Management. - : Blackwell Publishing Ltd.. - 0966-0429 .- 1365-2834. ; 5:6, s. 341-349
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Tidskriftsartikel (refereegranskat)abstract
- Although effective pain treatment is available for both cancer-related pain and acute post-operative pain, many patients suffer unnecessarily. The aim of this study was to evaluate post-operative patients' pain management. A descriptive survey study was conducted in a 460-bed acute hospital in the southwestern part of Sweden. One hundred post-operative inpatients, on their second post-operative day, took part in the study. They were consecutively selected from six surgical wards. Data were collected using an interview questionnaire designed by the American Pain Society and analysed by descriptive and inferential statistics. At the time of the interview, 29 of the patients reported moderate to severe pain. Regarding the patients' worst pain experienced during the last 24 h, 79 of them reported moderate to very severe pain. Significant correlations were found between reported poor pain relief after pain medication and high intensity of pain both within the last 24 h and at the time of the interview. Eighty-three patients were satisfied with the way nurses treated their pain, while 64 patients were satisfied with the way physicians treated their pain. However, the higher the pain intensity experienced by the patients the less satisfied they were. The fact that patients do not know what kinds of relief are available may be one reason for the patients expressing satisfaction despite being in pain, another that the patients judge the kindness of the staff rather than their way of treating the pain. The field of pain management is rapidly changing requiring professional knowledge and experience in order to ensure pain management of good quality.
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- Kleywegt, GJ, et al.
(författare)
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The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 angstrom resolution, and a comparison with related enzymes
- 1997
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Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - 0022-2836. ; 272:3, s. 383-397
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Tidskriftsartikel (refereegranskat)abstract
- Cellulose is the most abundant polymer in the biosphere. Although generally resistant to degradation, it may be hydrolysed by cellulolytic organisms that have evolved a variety of structurally distinct enzymes, cellobiohydrolases and endoglucanases, for this purpose. Endoglucanase I (EG I) is the major endoglucanase produced by the cellulolytic fungus Trichoderma reesei, accounting for 5 to 10% of the total amount of cellulases produced by this organism. Together with EG I from Humicola insolens and T. reesei cellobiohydrolase I (CBH I), the enzyme is classified into family 7 of the glycosyl hydrolases, and it catalyses hydrolysis with a net retention of the anomeric configuration.The structure of the catalytic core domain (residues 1 to 371) of EG I from T. reesei has been determined at 3.6 A resolution by the molecular replacement method using the structures of T. reesei CBH I and H. insolens EG I as search models. By employing the 2-fold non-crystallographic symmetry (NCS), the structure was refined successfully, despite the limited resolution. The final model has an R-factor of 0.201 (Rfree 0.258).The structure of EG I reveals an extended, open substrate-binding cleft, rather than a tunnel as found in the homologous cellobiohydrolase CBH I. This confirms the earlier proposal that the tunnel-forming loops in CBH I have been deleted in EG I, which has resulted in an open active site in EG I, enabling it to function as an endoglucanase. Comparison of the structure of EG I with several related enzymes reveals structural similarities, and differences that relate to their biological function in degrading particular substrates. A possible structural explanation of the drastically different pH profiles of T. reesei and H. insolens EG I is proposed.
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- Mackenzie, L F, et al.
(författare)
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Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 angstrom resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate
- 1998
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Ingår i: Biochemical Journal. - : Portland Press Ltd.. - 0264-6021 .- 1470-8728. ; 335, s. 409-416
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Tidskriftsartikel (refereegranskat)abstract
- Cellulose is the major polysaccharide component of the plant cell wall and the most abundant naturally produced macromolecule on Earth. The enzymic degradation of cellulose, by cellulases, is therefore of great environmental and commercial significance. Cellulases are found in 12 of the glycoside hydrolase families classified according to their amino acid sequence similarities. Endoglucanase I (Cel7B), from the soft-rot fungus Humicola insolens, is a family 7 enzyme. The structure of the native form of Cel7B from H. insolens at 2.2 Å resolution has been solved by molecular replacement using the known Trichoderma reesei cellobiohydrolase I [Divne, Ståhlberg, Reinikainen, Ruohonen, Pettersson, Knowles, Teeri and Jones (1994) Science265, 524–528] structure as the search model. Cel7B catalyses hydrolysis of the β-1,4 glycosidic linkages in cellulose with net retention of anomeric configuration. The catalytic nucleophile at the active site of Cel7B has been identified as Glu-197 by trapping of a 2-deoxy-2-fluorocellotriosyl enzyme intermediate and identification of the labelled peptide in peptic digests by tandem MS. Site-directed mutagenesis of both Glu-197 and the prospective catalytic acid, Glu-202, results in inactive enzyme, confirming the critical role of these groups for catalysis.
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