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Versorgung.Interaktiv.Gestalten : gute Interaktionsarbeit in digital unterstützten Versorgungsprozessen : Ergebnisse des Modellprojekts ProDigA (2023)

Greuèl, Marius [VerfasserIn]

Saarbrücken : Institut für Sozialforschung und Sozialwirtschaft (iso) e.V.

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Keywords: Forschungsbericht ; Gesundheitswesen ; Nervendegeneration ; Krankenpflege ; Hauspflege ; Sekundärkrankheit ; Ambulanter Hilfs- und Pflegedienst ; Pflegeperson ; App ; Case Management ; Portal ; Prozessorganisation

Type of Medium: Online Resource

Pages: 1 Online-Ressource (132 Seiten, 4,37 MB) , Illustrationen

Series Statement: iso-Report Nr. 7

URL: https://www.iso-institut.de/iso-reports/

URL: https://edocs.tib.eu/files/e01fb24/1881532070.pdf

Language: German

Note: Förderkennzeichen BMBF 02L18A130-135 , Verbundnummer 01212224 , Laufzeit: 01.04.2020 bis 31.03.2023 , Das Vorhaben „ProDigA - Digital unterstützte Interaktionsarbeit“ (FKZ: 02L18A130) wurde im Rahmen des Programms „Zukunft der Arbeit“ vom Bundesministerium für Bildung und Forschung (BMBF) und dem Europäischen Sozialfonds (ESF) gefördert , Literaturangaben

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Serological properties and processing in Escherichia coli K12 of OmpV fusion proteins of Vibrio cholerae (1986)

Pohlner, Johannes ; Meyer, Thomas F. ; Manning, Paul A.

Springer

Molecular genetics and genomics 205 (1986), S. 501-506

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ISSN: 1617-4623

Keywords: Signal sequence ; Antigenic epitopes ; Outer membrane protein ; Immunogenicity

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Fusion proteins comprising the amino-terminal 99 amino acids of the bacteriophage MS2 replicase and various portions of OmpV a major outer membrane protein of Vibrio cholerae were expressed in Escherichia coli K12. These fusions were expressed under the control of the PL promoter of bacteriophage λ, and expression was controlled using a cIts repressor. Fusions occurring within the secretory signal sequence of OmpV gave rise to the production of mature OmpV. The efficiency, however, decreased with progressive deletion of the signal sequence within the fusions. The reactivity of various OmpV fusions with antisera raised against purified OmpV and whole bacteria demonstrated the existence of two antigenic domains: one present in the denatured form and another in the membrane-associated form of OmpV. These domains correspond to markedly hydrophilic regions of the protein as would be predicted for surface-exposed epitopes.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00338089

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