| 1. |
- Akselsson, Roland, et al.
(author)
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Multidisciplinary Research on Integration of Human Factors and Production Concepts such as TQM - A Participatory Discussion Session
- 1999
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In: Proceedings of the Conference on TQM and Human Factors. - 9172195207 ; 2, s. 439-448
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Conference paper (peer-reviewed)abstract
- A discussion session where the conference participants are invited to participate is planned. One topic for the session is to discuss experiences of multidisciplinary research on integration of human factors and different production concepts applied in change processes within Swedish companies. An important question that the discussion will focus on is: How to get high quality in multidisciplinary research? Another topic is to discuss how people from different disciplines in the companies interact with each other and with the researchers. Researchers from the centre Change@Work at Lund University in Sweden will present some of their experiences from several years of multidisciplinary research in companies. As a background the research questions within Change@Work are presented below. Discussions during the workshop will be performed according to methods used by the researchers in their research in the companies. All discussion will be documented and later sent to all workshop participants.
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| 2. |
- Bergman, Anna Carin, et al.
(author)
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dUTPase from the Retrovirus Equine Infectious Anemia Virus: High-Level Expression in Escherichia coli and Purification
- 1995
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In: Protein Expression and Purification. - : Elsevier BV. - 1046-5928. ; 6:3, s. 379-387
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Journal article (peer-reviewed)abstract
- Deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase, EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, and plays important roles in nucleotide metabolism and DNA replication. The dUTPase gene of the retrovirus equine infectious anemia virus (EIAV) was cloned and overexpressed in Escherichia coli using the T7 RNA polymerase expression system. The recombinant vector (pET-3a/EDU), constructed by mutagenic PCR, was transformed into E. coli BL21(DE3) pLysS cells, resulting in expression of EIAV dUTPase at about 40% of the extracted protein, This level of overproduction is very high compared to previous reports on heterologous expression of dUTPases in E. coli. A one-step purification procedure using phosphocellulose chromatography results in a homogeneous preparation of the enzyme in a yield of 45 mg liter−1 of bacterial culture. The purified EIAV dUTPase, run on a sodium dodecyl sulfate-polyacrylamide gel electrophoresis, shows an apparent molecular mass of 15.1 kDa in accordance with the gene structure. The isoelectric point (pI) was determined to 5.6. Gel filtration under nondenaturating conditions gives a retention volume corresponding to a molecular mass of 40.8 kDa, suggesting a trimeric organization of the enzyme. The amino acid composition and amino-terminal sequence of the recombinant dUTPase are in agreement with predictions from the DNA sequence.
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| 3. |
- Bergman, Anna-Carin, et al.
(author)
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Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1
- 1998
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In: FEBS Letters. - 1873-3468. ; 441:2, s. 327-330
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Journal article (peer-reviewed)abstract
- Kinetic properties of the monomeric enzyme dUTPase from herpes simplex virus type 1 (HSV) were investigated and compared to those previously determined for homotrimeric dUTPases of bacterial and retroviral origins. The HSV and Escherichia coli dUTPases are equally potent as catalysts towards the native substrate dUTP with a kcat/KM of about 107 M-1 s-1 and a KM of 0.3 μM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificity towards the racemic substrate analogue dUTPαS (2'-deoxyuridine 5'-(α-thio)triphosphate), suggesting that they have identical reaction mechanisms.
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| 4. |
- Bergman, Kerstin, et al.
(author)
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I begynnelsen var ordet - men hur är det idag?
- 1997
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In: Litteraturens ställning. - 9172032480 ; , s. 34-47
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Book chapter (other academic/artistic)abstract
- About the functions and interpretative consequences of cover art on literary fiction.
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| 5. |
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| 6. |
- Monemar, Bo, et al.
(author)
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Radiative recombination in In0.15Ga0.85N/GaN multiple quantum well structures
- 1999
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In: MRS Internet Journal of Nitride Semiconductor Research. - 1092-5783. ; 4:16
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Journal article (peer-reviewed)abstract
- We present a study of the radiative recombination in In0.15Ga0.85N/GaN multiple quantum well samples, where the conditions of growth of the InGaN quantum layers were varied in terms of growth temperature (< 800 degrees C) and donor doping. The photoluminescence peak position varies strongly (over a range as large as 0.3 eV) with delay time after pulsed excitation, but also with donor doping and with excitation intensity. The peak position is mainly determined by the Stark effect induced by the piezoelectric field. In addition potential fluctuations, originating from segregation effects in the InGaN material, from interface roughness, and the strain fluctuations related to these phenomena, play an important role, and largely determine the width of the emission. These potential fluctuations may be as large as 0.2 eV in the present samples, and appear to be important for all studied growth temperatures for the InGaN layers. Screening effects from donor electrons and excited electron-hole pairs are important, and account for a large part of the spectral shift with donor doping (an upward shift of the photoluminescence peak up to 0.2 eV is observed for a Si donor density of 2 x 10(18) cm(-3) in the well), with excitation intensity and with delay time after pulsed excitation (also shifts up to 0.2 eV). We suggest a two-dimensional model for electron- and donor screening in this case, which is in reasonable agreement with the observed data, if rather strong localization potentials of short range (of the order 100 Angstrom) are present. The possibility that excitons as well as shallow donors are impact ionized by electrons in the rather strong lateral potential fluctuations present at this In composition is discussed.
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| 7. |
- Olofsson, Hans, et al.
(author)
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A thin molecular shell around the carbon star TT Cyg
- 1998
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In: ASTRONOMY AND ASTROPHYSICS. - : SPRINGER VERLAG. - 0004-6361. ; 330:1, s. L1-L4
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Journal article (peer-reviewed)abstract
- Interferometric CO(J=1 --> 0 and 2 --> 1) observations reveal a remarkably thin shell of molecular gas around the carbon star TT Cyg, width/radius less than or similar to 1." 3/34 " approximate to 0.04. It expands at approximate to 13 km s(-1), and contai
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| 8. |
- Vertessy, Beata G., et al.
(author)
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The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase
- 1998
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In: FEBS Letters. - 1873-3468. ; 421:1, s. 83-88
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Journal article (peer-reviewed)abstract
- The molecular mechanism of substrate analogue interaction with Escherichia coli dUTPase was investigated, using the non-hydrolyzable 2'-deoxyuridine 5'-(α,β-imido)triphosphate (α,β-imido-dUTP). Binding of this analogue induces a difference in the far UV circular dichroism (CD) spectrum arguing for a significant change in protein conformation. The spectral shift is strictly Mg2+-dependent, does not appear with dUDP instead of α,β-imido-dUTP and is not elicited if the flexible C-terminal arm is deleted from the protein by limited tryptic digestion. Involvement of the C-terminal arm in α,β-imido-dUTP binding is consistent with the finding that this analogue protects against tryptic hydrolysis at Arg-141. Near UV CD of ligand-enzyme complexes reveals a characteristic difference in the microenvironments of enzyme-bound dUDP and α,β-imido-dUTP, a difference not observable in C-terminally truncated dUTPase. The results suggest that (i) closing of the active site during the catalytic cycle, through the movement of the C-terminal arm, requires the presence of the complete triphosphate moiety of the substrate in complex with Mg2+, and (ii) after catalytic cleavage the active site pops open to facilitate product release.
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