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Träfflista för sökning "WFRF:(Svensson R) srt2:(1985-1989)"

Sökning: WFRF:(Svensson R) > (1985-1989)

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1.
  • Ericson, Mats O, et al. (författare)
  • The forces of ankle joint structures during ergometer cycling.
  • 1985
  • Ingår i: Foot & ankle. - : SAGE Publications. - 0198-0211. ; 6:3, s. 135-42
  • Tidskriftsartikel (refereegranskat)abstract
    • The ankle joint moment, joint compressive force, and Achilles tendon force obtained during ergometer cycling were calculated by using a quartz force-measuring transducer mounted on the pedal. Six healthy subjects rode in 11 different ways at different workloads, pedalling rates, saddle heights, and pedal foot positions. The mean maximum dorsiflexing load moment about the ankle joint during standardized ergometer cycling was calculated to 30.9 nm. The mean ankle joint compressive force and mean Achilles tendon force measured 1008 N (1.4 times body weight) and 762 N (1.1 times body weight), respectively. The ankle joint moment was significantly changed by a change of workload or pedal foot position.
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2.
  • Nilsson, B, et al. (författare)
  • A simplified assay for the detection of C3a in human plasma employing a monoclonal antibody raised against denatured C3.
  • 1988
  • Ingår i: JIM - Journal of Immunological Methods. - 0022-1759 .- 1872-7905. ; 107:2, s. 281-287
  • Tidskriftsartikel (refereegranskat)abstract
    • A monoclonal antibody raised against SDS-denatured C3 was shown to react with both solid-phase C3a and unfragmented C3. However, in the fluid phase the antibody was found to bind only to C3a and not to native C3. These findings indicated that the antibody could be used in an assay to detect C3a in human EDTA-plasma without prior separation of C3a from native C3. A simple and rapid competition ELISA was developed which monitored soluble C3a. 200 microliter of C3a (8 ng) was absorbed to plastic wells over night at 4 degrees C. Thereafter, 50 microliter of sample and 50 microliter of constant amounts of monoclonal antibody conjugated with beta-galactosidase, were incubated for 60 min at 37 degrees C. After washing, the colour reaction was started by adding nitrophenyl-galactopyridine to the wells. The microtitre plate was incubated at 37 degrees C for 30 min and the staining intensity was quantified at 405 nm. The assay detected both C3a and C3ades arg. A strong correlation was obtained between the new technique and an RIA which used an acid precipitation step for the separation of C3a prior to the determination of C3a (r = 0.9). Significantly higher levels of C3a were detected both in plasma from patients with immune complexes (93 +/- 9 ng/ml; P less than 0.1) and in plasma from patients treated in blood oxygenators (140 +/- 19 ng/ml; P less than 0.05) than in plasma from normal subjects (74 +/- 4 ng/ml). The results were not affected by repeated freezing and thawing of the plasma samples.
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3.
  • Nilsson, Bo, et al. (författare)
  • Distinctive expression of neoantigenic C3(D) epitopes on bound C3 following activation and binding to different target surfaces in normal and pathological human sera
  • 1989
  • Ingår i: Molecular Immunology. - : Elsevier BV. - 0161-5890 .- 1872-9142. ; 26:4, s. 383-390
  • Tidskriftsartikel (refereegranskat)abstract
    • Binding of C3 to sheep erythrocytes in a serum-free milieu (EAC14oxy2, EAC142) has previously been shown to mimic the antigenic change that occurs upon denaturation of C3 in sodium dodecyl sulphate (SDS), whereby neoantigenic C3(D) epitopes are exposed. The present paper deals with C3 bound to various target surfaces which are known to modulate the functional properties of C3 in different ways. Bound C3 fragments on serum-treated human aggregated gammaglobulin, zymosan, rabbit and sheep erythrocytes, and on circulating immune complexes isolated from sera of patients with rheumatoid arthritis and systemic lupus erythematosus, were shown to be mainly in the iC3b form. By RIAs, employing polyclonal antibodies, the range of C3(D) antigenic epitopes of 125I-labelled SDS denatured C3 expressed by the particle-bound iC3b was monitored. The physiologically bound iC3b on all tested particles expressed wide ranges of C3(D) epitopes and each type of particle-bound C3 exposed its individual range. By competition ELISA specific C3(D)α epitopes were monitored, employing monoclonal antibodies. A distinct difference in the expression of these epitopes was observed in iC3b bound to various test particles in the presence of normal serum and in iC3b present on circulating immune complexes from pathological sera. Considering that the neoantigenic C3(D) epitopes have been shown to be associated with different functions of C3, the distinctive antigenic expression of each type of serum-treated particle might reflect different functional forms of the protein. 
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4.
  • Nilsson, B, et al. (författare)
  • Production of mouse monoclonal antibodies that detect distinct neoantigenic epitopes on bound C3b and iC3b but not on the corresponding soluble fragments.
  • 1987
  • Ingår i: Molecular Immunology. - 0161-5890 .- 1872-9142. ; 24:5, s. 487-494
  • Tidskriftsartikel (refereegranskat)abstract
    • Polyclonal antibodies raised in rabbits against sodium dodecyl sulphate (SDS)-denatured and reduced human complement factor C3 have in recent studies been shown to lack any reactivity towards native C3 but to react with antigens distinctly expressed by SDS-denatured C3 (C3(D) antigens). These antigens are also neoantigens specific for physiologically bound C3 and appear to be involved in the interaction of C3 with other complement components. The present investigation deals with production of mouse monoclonal antibodies against C3(D) antigens. To accomplish this two different immunization and screening procedures employing C3 preparations of known C3(D) expression were tested. From each group 14 clones were randomly selected and the reactivity of these and of a control group of 14 additional monoclonal anti-human C3 antibody preparations raised against native soluble C3 and C3b, was investigated in ELISA and immunoblotting. The procedure which employed denatured reduced C3 as both immunogen as well as screening antigen was shown to be superior for obtaining anti-C3(D) antibodies. Altogether 16 clones producing antibodies against C3(D) antigens were found. All of them bound to the C3 alpha-chain, 14 to C3c and one to C3d, and eight monoclonal antibodies specific for neoantigens of C3(D) type on bound C3b and/or iC3b were obtained. The majority of these detected neoantigenic epitopes in the 25,000 N-terminal fragment of the C3 alpha-chain specifically exposed by bound iC3b, but one monoclonal antibody was specific for the 36,000 C-terminal alpha-chain fragment and for both bound C3b and iC3b.
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5.
  • Ulfvarson, U, et al. (författare)
  • Effects of exposure to vehicle exhaust on health
  • 1987
  • Ingår i: Scandinavian Journal of Work, Environment and Health. - : Scandinavian Journal of Work, Environment and Health. - 0355-3140 .- 1795-990X. ; 13:6, s. 505-512
  • Tidskriftsartikel (refereegranskat)abstract
    • Exposure to combustion engine exhaust and its effect on crews of roll-on roll-off ships and car ferries and on bus garage staff were studied. The peak concentrations recorded for some of the substances studied were as follows: total particulates (diesel only) 1.0 mg/m3, benzene (diesel) 0.3 mg/m3, formaldehyde (gasoline and diesel) 0.8 mg/m3, and nitrogen dioxide (diesel) 1.2 mg/m3. The highest observed concentration of benzo(a)pyrene was 30 ng/m3 from gasoline and diesel exhaust. In an experimental study volunteers were exposed to diesel exhaust diluted with air to achieve a nitrogen dioxide concentration of 3.8 mg/m3. Pulmonary function was affected during a workday of occupational exposure to engine emissions, but it normalized after a few days with no exposure. The impairment of pulmonary function was judged to have no appreciable, adverse, short-term impact on individual work capacity. In the experimental exposure study, no effect on pulmonary function was observed. Analyses of urinary mutagenicity and thioether excretion showed no sign of exposure to genotoxic compounds among the occupationally exposed workers or among the subjects in the experimental study.
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