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- Abrahamsson, K, et al.
(författare)
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Marine algae - a source of trichloroethylene and perchloroethylene
- 1995
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Ingår i: Limnology and Oceanography. - 0024-3590 .- 1939-5590. ; 40:7, s. 1321-1326
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Tidskriftsartikel (refereegranskat)abstract
- Our results show the natural production of two olefins, trichloroethylene and perchloroethylene, by various marine macroalgae and a microalga. We found significant difference in the ability of the algae to produce these compounds. The production rates for trichloroethylenevaried between 0.022 and 3,400 ng g-l fresh wt (FW)h-l and were generally higher than those for perchloroethylene(0.0026-8.2 ng g-l FW h-l). The two subtropicalalgae, Asparagopsis taxiformis and Falkenbergia hillebrandii,showed the highest formation rates. One axenicmarine red microalga, Porphyridium purpureum, was alsotested and it could also produce trichloroethylene and perchloroethylene.The measured rates suggest that the emissionof trichloroethylene and perchloroethylene from theoceans to the atmosphere may be of such a magnitude thatit cannot be neglected in the global atmospheric chlorinebudget.
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- Ekdahl, K N, et al.
(författare)
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Increased phosphate content in complement component C3, fibrinogen, vitronectin, and other plasma proteins in systemic lupus erythematosus : covariation with platelet activation and possible association with thrombosis.
- 1997
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Ingår i: Arthritis and Rheumatism. - 0004-3591 .- 1529-0131. ; 40:12, s. 2178-2186
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Tidskriftsartikel (refereegranskat)abstract
- OBJECTIVE: To investigate whether extracellular phosphorylation of plasma proteins takes place in vivo in patients with systemic lupus erythematosus (SLE), to determine possible correlations between phosphate levels and clinical and/or laboratory parameters, and to identify individual phosphorylated plasma proteins.METHODS: Sera from SLE patients were analyzed for total amounts of protein-bound phosphate by a colorimetric technique, and for levels of beta-thromboglobulin by radioimmunoassay. In addition, the ability of these sera to activate platelets, resulting in the release of protein kinase, was tested using an assay in which platelet-rich plasma from healthy blood donors was incubated with sera or immune complexes from SLE patients. In this assay, [gamma-32P]ATP was added, and 32P-labeled C3 was quantified. Phosphate in individual proteins was detected by Western blot analysis.RESULTS: 32P-labeled, activated platelets were able to phosphorylate exogenously added proteins, without the addition of ATP or cations. Platelet-rich plasma from healthy blood donors became activated by sera or by polyethylene glycol-precipitated immune complexes from patients with SLE, which led to the extracellular phosphorylation of plasma proteins, exemplified in the C3 assay. The phosphate content in plasma proteins was increased in SLE patients with previous thrombosis. The degree of phosphorylation increased up to 3-fold in serial samples obtained from 2 SLE patients during periods of disease exacerbation. Substantial phosphate increases were seen in C3 and fibrinogen. The changes were linked to platelet activation because of the observed covariation with the levels of beta-thromboglobulin.CONCLUSION: In SLE patients, the phosphate content in plasma proteins (including C3 and fibrinogen) increases due to platelet activation.
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- Ekdahl, K N, et al.
(författare)
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Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase. Inhibition of factor I-mediated cleavage of C3b.
- 1995
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Ingår i: Journal of Immunology. - 0022-1767 .- 1550-6606. ; 154:12, s. 6502-6510
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Tidskriftsartikel (refereegranskat)abstract
- Phosphorylation of C3 in vitro has been shown previously to lead to significantly altered function of the protein. Platelets are known to contain and release considerable amounts of protein kinases and ATP, which are prerequisites for protein phosphorylation. The aim of the present study was to investigate whether C3 is phosphorylated extracellularly by human platelets. Platelet-rich plasma was stimulated by human aggregated gamma-globulin or ADP. The remaining cells were removed by centrifugation, and the plasma was incubated with [gamma-32P]ATP. After precipitation with Sepharose-bound Abs to C3c followed by SDS-PAGE, it was shown that C3 was phosphorylated in the alpha-chain by a protein kinase dependent on Mn2+, Ca2+, or Mg2+ ions. The supernatant from washed, activated platelets was incubated with purified C3 or soluble or activated thiol Sepharose-bound C3b, together with [gamma-32P]ATP. Phosphorylation was seen in the alpha-chain of C3, and to the same extent in the alpha'-chain of both C3b preparations. The analysis of acid hydrolysate demonstrated that C3 contained 32P-labeled Thr and 32P-labeled Ser. After extensive proteolysis with trypsin, the major phosphorylation site was located to a peptide of 3 to 4 kDa that was bound to the activated thiol Sepharose via the free sulphydryl group in the C3d fragment. Incubation of phosphorylated C3b with factors I and H showed that phosphorylation inhibited the cleavage of the alpha'-chain of C3b. The results in this study suggest that phosphorylation is a regulator of C3 during platelet activation induced, for example, by immune complexes.
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- Gong, J, et al.
(författare)
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Tubing loops as a model for cardiopulmonary bypass circuits : both the biomaterial and the blood-gas phase interfaces induce complement activation in an in vitro model.
- 1996
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Ingår i: Journal of Clinical Immunology. - 0271-9142 .- 1573-2592. ; 16:4, s. 222-223
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Tidskriftsartikel (refereegranskat)abstract
- We describe here a model for the study of blood/surface and blood/air interaction as encountered in cardiopulmonary bypass (CPB) circuits. Polyethylene tubing was filled with serum or blood and closed end to end into loops whereby the volume of the remaining air bubble was inversely varied with respect to that of the fluid. The loops were rotated vertically in a water bath at 37 degrees C. The profiles of C3a, iC3, and TCC generation were similar to those observed at surgery, involving CPB. Soluble heparin and heparan sulfate inhibited both C3a and TCC formation, but surface-conjugated heparin had only a minor effect. Binding of C3 and/or C3 fragments to the heparin surface was much reduced compared to the amine matrix to which heparin was linked, but compared with the polyethylene surface the effect was less pronounced. These data suggest that, in addition to the biomaterial surface, the blood-gas interface seems to play an important role in the activation of complement and that this activation is inhibitable by high concentrations of soluble glucose aminoglycans.
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- Gustafsson, Anders, et al.
(författare)
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Working without Matrices - How Volvo Does it
- 1998
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Ingår i: the Fourth International QFD Symposiums in Sydney, Australia.
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Tidskriftsartikel (refereegranskat)abstract
- This paper illustrates how Volvo tries to save time in QFD projects by adapting the methodology to the specific situations where QFD is used at Volvo. Specifically, the paper illustrates Volvo's aim to always find engineering characteristics that can be measured objectively and are correlated with specific customer needs. This way Volvo can save considerable time by omitting the relationship matrix. The underlying ideas presented in the paper are supported by an empirical example, the Volvo T4, which is a high performance car based on Volvo's S40 and V40 models
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