| 1. |
- Harris, A.S., et al.
(författare)
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Effect of viscosity on the pharmacokinetics and biological response to intranasal desmopressin.
- 1989
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Ingår i: Journal of Pharmaceutical Sciences. - : Elsevier BV. - 0022-3549. ; 78:6, s. 470-471
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Tidskriftsartikel (refereegranskat)abstract
- he effect of viscosity on the nasal absorption and biological response to desmopressin was studied in humans. Nasal solutions of desmopressin with and without the addition of 0.25% (w/v) methylcellulose were administered by a precompression nasal spray pump to 10 volunteers. Plasma levels of desmopressin were assayed by radioimmunoassay and the biological response was measured by determination of the antihemophilia factors (Factor VIII and von Willebrand factor). The results showed that the addition of methylcellulose produced a more sustained and slower absorption, with a longer time to maximum plasma concentration (tmax). However, the areas under the plasma concentration—time curve were not different, indicating a similar total bioavailability. The biological response showed a similar effect. Peak Factor VIII activity was not different, but the presence of methylcellulose produced a slower onset of activity. These findings indicate that although the addition of a viscous agent to nasal formulations may produce a more sustained effect, it delays the onset of activity and no enhancement is achieved in the total bioavailability.
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| 2. |
- Hansson, Ulla-Britt, et al.
(författare)
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IgG with a deviant conformation in serum and synovial fluid from rheumatoid arthritis patients
- 1985
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Ingår i: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 22:1, s. 27-32
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Tidskriftsartikel (refereegranskat)abstract
- Specific rabbit antisera were prepared against an IgG with a special conformation (IgG spec.) previously detected in some sera from patients with rheumatoid arthritis. The antibodies had no affinity to normal human IgG and were not anti-idiotypic to human rheumatoid factor. The affinity of IgG spec, to the antibodies could not be explained by an antiglobulin activity to rabbit IgG. The amount of protein with affinity to immobilized specific IgG F(ab′)2 of the antibodies was determined in serum and synovial fluid from patients with various joint diseases. A relationship between the content of IgG spec, and the diagnosis of seropositive rheumatoid arthritis was found on analysis of serum samples. IgG spec, also occurred in synovial fluid from some individuals with seropositive rheumatoid arthritis. Differences in the serum content of IgG spec, could not be explained by differences in the normal IgG content. Circular dichroism analysis of isolated IgG spec, showed that in the region(s) close to tyrosine residue(s) this polyclonal protein had similarities to heat-aggregated IgG.
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| 3. |
- Ohlin, Mats, et al.
(författare)
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Human monoclonal antibodies against a recombinant HIV envelope-antigen produced by primary in vitro immunization. Characterization and epitope mapping.
- 1989
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Ingår i: Immunology. - 0019-2805. ; 68:3, s. 325-331
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Tidskriftsartikel (refereegranskat)abstract
- Peripheral blood lymphocytes from healthy, HIV sero-negative blood donors have been in vitro immunized using penv9, a recombinant fragment of the envelope of HIV-1. This primary in vitro immunization followed by Epstein-Barr virus (EBV) transformation and somatic cell fusion subsequently gave rise to several specific anti-penv9 monoclonal antibodies (MO28, MO30 and MO43) of μ isotype. The hybridomas have been kept in culture for over 6 months and the antibody productivity for MO30 was measured to 18 μg × (24 hr × 106 cells)-1. The fine specificity of the antibodies was mapped by a peptide inhibition enzyme immunoassay, using overlapping synthetic pentadeca peptides covering the whole penv9. These human monoclonal antibodies exhibited a similar epitope specificity directed against a non-sequential determinant, including the amino acids 632–646, 677–681 and 687–691. This specificity is very rarely found in immune sera from sero-positive patients and presently not reported in human monoclonal antibodies derived from in vivo immunized individuals, indicating that different antibody specificities can be obtained by the in vitro immunization technology. These human monoclonal antibodies did not neutralize HIV. The results presented here demonstrate the feasability of generating human monoclonal antibodies against HIV by primary in vitro immunizations, thereby avoiding the use of lymphocytes derived from infected patients when human monoclonal antibodies for therapeutic purposes are to be produced.
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