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- Carlsson, Maria E., 1958-, et al.
(författare)
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Qualitative analysis of the questions raised by patients with gynecologic cancers and their relatives in an educational support group.
- 1999
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Ingår i: Journal of Cancer Education. - 0885-8195 .- 1543-0154. ; 14:1, s. 41-46
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Tidskriftsartikel (refereegranskat)abstract
- BACKGROUND People's knowledge of cancer is generally inadequate to help them cope with a diagnosis of cancer. Educational support groups may allow cancer patients to receive information they want that is normally not covered in the individual clinical encounter. It was desired to identify the content of such information as reflected in the questions asked by cancer patients and their relatives in such support groups. METHOD The 329 questions asked by 41 patients and 11 of their relatives in 40 group sessions were analyzed and categorized. RESULTS The categories found are described. Almost 100 questions could be allocated to the category "the illness," of which the most common was, "Is cancer hereditary?" The questions made it clear that the patients had a wish and a need to understand cancer. CONCLUSION An educational support group provides a complement to, and not a substitute for, the clinical provision of medical information.
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| 2. |
- Jendeberg, L, et al.
(författare)
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Engineering of Fc(1) and Fc(3) from human immunoglobulin G to analyse subclass specificity for staphylococcal protein A.
- 1997
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Ingår i: JIM - Journal of Immunological Methods. - 0022-1759 .- 1872-7905. ; 201:1, s. 25-34
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Tidskriftsartikel (refereegranskat)abstract
- A system for production of recombinant Fc fragments of human IgG in Escherichia coli has been developed to allow for structural and functional studies of human Fc. The genes for the Fc fragments of human IgG subclasses 1 and 3, designated Fc(1) and Fc(3), were cloned from a human spleen cDNA library. The interactions to Staphylococcal protein A (SpA), a bacterial Fc receptor, that interacts with human IgG-Fc(1), but not with human IgG-Fc(3), were analyzed. To corroborate the involvement of amino acid residues in Fc, responsible for these differences in binding, two Fc variants were constructed; Fc(1(3)) and Fc(3(1)), each containing an isotypic dipeptide substitution. Production levels in E. coli of 1-10 mg/l of secreted Fc proteins, covalently linked as dimers, were routinely obtained. SpA-binding analyses of all four Fc variants using biosensor technology, showed that Fc(1) and Fc(3(1)) interact with SpA, while Fc(3) and Fc(1(3)) lack detectable SpA binding. The rendered SpA binding of the Fc variant Fc(3(1)), is concluded to result from the introduced dipeptide substitution (R435H, F436Y). The results demonstrate that the Fc expression system efficiently can be used in Fc engineering.
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