| 1. |
- Andersen, Poul, et al.
(author)
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Tackling Dynamics in Business Networks
- 1994
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In: 10th Annual IMP Conference, Groningen. - Groningen : University of Groningen, Faculty of Management & Organization.
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Conference paper (peer-reviewed)
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| 2. |
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En väg med historia
- 1992
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In: En väg med historia. - Linköping : Riksantikvarieämbetet. ; , s. 9-12
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Editorial collection (other academic/artistic)
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| 3. |
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| 4. |
- Fröjmark, Anders
(author)
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Mirakler och helgonkult : Linköpings biskopdöme under senmedeltid
- 1992
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Doctoral thesis (other academic/artistic)abstract
- This work studies the introduction of three new cults of saints in the Linköping Bishopric during the Late Middle Ages. Two of them were based at Vadstena Convent: the Holy Bridgel (Birgitta, d. 1373) cult which had its beginning in 1374 and the cult of Katarina Ulfsdotter (d. 1381), which started during the 1410's. The third, the cult of Bishop Nils Hermansson (d. 1391), which originated at the latest in I40l. was associaled w ith the cathedral in Linköping.The introduction of a saint's cult may be relaled to the need of many people in medieval society for healing and protection. The tales about the saint's posthumous miracles played a key role in the introductory phase of the cults. In the dissertation such tales are used as the foundation for the analysis of the varied geographic and social patterns of distnbution of the three cults.The cult of the Holy Bridget was as much an intemational as a Swedish cult. The other cults studied were two of manv attempts to ride on the wave created by the successes of the Bridget cult. They may furthermore be regarded a response to various types of crises which the sponsoring institutions experienced.
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| 5. |
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| 6. |
- Lavö, B, et al.
(author)
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Fc receptor function and circulating immune complexes in gluten sensitive enteropathy - possible significance of serum IgA
- 1991
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In: Gut. - : BMJ. - 0017-5749 .- 1468-3288. ; 32, s. 876-880
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Journal article (peer-reviewed)abstract
- The capacity to clear IgG containing immune complexes from the circulation was studied in patients with coeliac disease (n = 13), dermatitis herpetiformis (n = 8), and coeliac disease with concomitant serum IgA deficiency (n = 4). A small group of patients with active ulcerative colitis (n = 4) was included as a bowel disease control group. Clearance was estimated by measuring the disappearance rate of a bolus dose of intravenously injected IgG coated autologous erythrocytes. The mean T1/2 of clearance was prolonged in both coeliac disease (86 (24) minutes) and dermatitis herpetiformis (111 (35) minutes), compared with healthy subjects (20 (5) minutes) and coeliac patients with concomitant serum IgA deficiency (T1/2 = 17 (6) minutes). Patients with ulcerative colitis had a prolonged clearance, with a T1/2 of 195 (63) minutes. Values of circulating immune complexes were measured by four assays; C1q binding and C3, IgG, and IgA containing immune complexes. C1q binding immune complexes were detected only in IgA deficient gluten sensitive enteropathy. Patients with coeliac disease and dermatitis herpetiformis had higher values of C3, IgG, and IgA containing immune complexes than control subjects and serum IgA deficient patients with coeliac disease. The clearance rate was inversely correlated to the amount of immune complexes for the subgroups of gluten sensitive enteropathy.
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| 7. |
- Nilsson Ekdahl, Kristina, et al.
(author)
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An improved method to study complement receptor-mediated function of the fixed macrophage system in vivo
- 1991
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In: Vox Sanguinis. - : Wiley. - 0042-9007 .- 1423-0410. ; 61:1, s. 47-52
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Journal article (peer-reviewed)abstract
- A method to coat unsensitized erythrocytes with fragments of C3 and C4 using autologous serum, in order to study complement receptor-dependent function of the fixed macrophage system, is presented. After incubation with serum under optimal conditions, at least 90% of the cells had C3b/iC3b deposited on the surface, with an average of 20 × 103 molecules per cell. Elimination of the coated cells by the fixed macrophage system was studied in 12 normal subjects. With a dose of 4.5 × 108 red cells injected, 75% of the cells were eliminated with a half-life of approximately 2.4 ± 0.3 min (n = 7). In subjects receiving ten times more cells, there was a rapid decrease in the amount of C3-coated cells, reaching a nadir with 85% remaining for 4–6 min, after which there was a gradual release of cells for another 20 min (n = 5). In absolute numbers, 3 × 108 of labeled cells were eliminated regardless of the dose injected. The coating procedure presented here is simple, does not introduce heterologous blood components and makes it possible to control the amount and the degree of fragmentation of the C3 and C4 deposited on the erythrocyte surface.
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| 8. |
- Nilsson Ekdahl, Kristina, et al.
(author)
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Generation of iC3 on the interphase between blood and gas
- 1992
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In: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 35:1, s. 85-91
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Journal article (peer-reviewed)abstract
- Earlier studies have shown that C3 can be denatured when blood comes in contact with a polystyrene surface. This study was undertaken to sec if similar denaturation of C3 occurs at the gas plasma interface which is found in all kinds of oxygenator used during cardio-pulmonary operations. An in vitro system consisting of gas bubbling through human blood, serum or plasma was used. The generation of C3a, as an indicator of complement activation, and iC3 and iC3 fragments were monitored. Both C3a and iC3/iC3 fragments levels were increased during bubbling. In contrast to the C3a level, no reduction in iC3/iC3 fragments formation was seen in the presence of EDTA, indicating that il was independent of complement activation. The rate of iC3/iC3 fragments generation was unaffected by the composition of the gas (pure oxygen, pure nitrogen or air), suggesting that the denaturation of C3 indeed occurred at the serum gas interface. C3 and iC3/iC3 fragments were isolated from bubbled EDTA-chelated serum by PEG precipitation and chromatography on FPLC, using a Mono S column and detected by two ELISAs, specific for native C3 and iC3/iC3 fragments. After 240 min approximately 20% of the total amount of C3 consisted of intact iC3 and it was confirmed that this population bound to human erythrocytes.
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| 9. |
- Nilsson Ekdahl, Kristina, et al.
(author)
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Inhibition of factor I by diisopropylfluorophosphate. Evidence of conformational changes in factor I induced by C3b and additional studies on the specificity of factor I
- 1990
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In: Journal of Immunology. - 0022-1767 .- 1550-6606. ; 144:11, s. 4269-4274
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Journal article (peer-reviewed)abstract
- The factor I-mediated cleavage of C3b, using factor H as a cofactor was completely inhibited by diisopropylfluorophosphate (DFP) when factor I and C3b were incubated with DFP before the addition of factor H. Inhibition, although to a lesser degree, was observed when factor H was present during DFP-exposure. No inhibition in factor I activity was seen when factor I and H were incubated with DFP either alone or together. It was also demonstrated that the 38-kDa subunit of factor I bound radiolabeled DFP when factor I and C3b together were exposed to DFP. These observations suggest that factor I interacts with C3b in a manner that exposes its catalytic site to DFP, an interaction that is independent of factor H. The inhibitory effect by DFP on factor I led us to further investigate the factor I cleavage products of iC3b, inasmuch as previous reports were ambiguous as to whether digestion occurs in the presence of DFP. Digestion of C3b bound to activated thiol Sepharose (ATS-C3b) in the presence of factor H at low pH and ionic strength and in serum by complement activation produced C3d,g- like fragments with apparent molecular mass of 41 and 43 kDa. These fragments were shown to have three different N-terminal and two different C-terminal ends. The major fragments had N-terminal sequences starting with Glu933, as shown by sequence determination. Traces of fragments extending beyond this point were also found, shown by Western blot analysis using a panel of mAb previously shown to bind to epitopes exposed within a region of C3 spanning residues 929 to 943, as well as a shorter fragment starting with Glu938. When digestion of C3b is carried out in the presence of DFP, the factor I level necessary for digestion is elevated and may explain how the first two cleavages producing iC3b but not the following giving C3d,g, can occur. The finding of several factor I cleavage sites in the C3d,g region of C3 demonstrates that factor I has a broad specificity, mainly for arginyl bonds. It has also been shown to digest a lysyl bond exposed in ATS- bound C3b.
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| 10. |
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