ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Blackwell Publishing Ltd  (4)
  • International Union of Crystallography (IUCr)  (1)
  • MDPI Publishing
  • 1995-1999  (3)
  • 1985-1989  (2)
Sammlung
Erscheinungszeitraum
Jahr
  • 1
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 11 (1995), S. 0 
    ISSN: 1574-695X
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: Abstract Mouse monoclonal antibody (mAb) Pgf-II specific for a 72-kDa major cell-surface protein (72K-CSP) derived from Porphyromonas gingivalis OMZ 409 was prepared. Immunoblotting analysis revealed that mAb Pgf-II reacted with 72K-CSP but not with 41-kDa fimbrial subunit protein (41K-fimbrilin) derived from P. gingivalis 381. Electron microscopic observation revealed that P. gingivalis OMZ 409 possessed peritrichous, thin fimbriae on their surface. Immunogold electron microscopy also demonstrated that mAb Pgf-II bound to the 72K-CSP examined with the gold particles arranged along the fibril array originating from the cell surface of the bacteria. These findings suggested that P. gingivalis 72K-CSP was identifiable as another fimbriae (termed Pg-II fimbriae) different from the fimbriae (termed Pg-I fimbriae) composed of a 41K-fimbrilin. Using multipin peptide synthesis technology, 102 sequential overlapping peptides covering the entire 514 amino-acid stretch of Pg-II fimbriae were synthesised. Seven immunodominant regions within Pg-II fimbrial protein molecule, which definitely reacted with the serum of patients with periodontal diseases, were detected.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract We previously established murine hybridomas producing a monoclonal antibody monospecific against three glucosyl-transferases (I, SI and S) of Streptococcus mutans which contribute to dental caries formation. Here, we developed a new immunochemical technique (cross-dot system) with which individual levels of glucosyltransferases expressed by S. mutans can be evaluated. We also examined glucosyltransferase production and in vitro artificial plaque formation by a reference strain and several clinical isolates of S. mutans. The findings indicate that the levels of glucosyltransferases produced greatly vary with the cells and the culture medium, and that the cells producing high levels of both glucosyltransferase-SI and glucosyltransferase-I enzymes may possess high in vitro artificial plaque forming ability. We suggest that the cross-dot system will be useful for estimating the cariogenic potential of S. mutans isolates.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    ISSN: 1750-3841
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Bluefin tuna oxymyoglobin (oxyMb) solutions were frozen either quickly at −80°C or slowly at −2O°C, thawed, and the metmyoglobin (metMb) to total myoglobin (Mb) ratio (metMb%) determined. When quick freezing was applied, autoxidation was clearly pH-dependent, with a minimum (metMb%, 15–40) at around pH 5.9–6.3. When slowly frozen and thawed, on the other hand, tuna Mb generally showed an extremely high metMb%. Freezing and thawing partially insolubilized tuna Mb, depending upon pH. The Mb showed the minimum ratio of insolubilization at pH 6–6.3 again. Insolubilization of tuna Mb was markedly accelerated by NaCl.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    ISSN: 1750-3841
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: The foot, opercular and visceral muscles were excised from the turban shell Batillus cornutus, and their heat-induced changes in toughness and ultrastructure were compared. When heated up to 30°C, the toughness of foot muscle decreased in the upper and middle regions, but increased in the lower region. The toughness of these three regions decreased at temperatures between 50-70°C, where collagen might be denatured. Some changes in toughness were also observed in the opercular muscle by heating up to 30°C, whereas the toughness of visceral muscle remained unchanged over a wide range of temperature. Transmission electron microscopy showed that the intrinsic structure of collagen fibrils in each muscle was lost at 60°C, with partial swelling.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    Digitale Medien
    Digitale Medien
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 702-703 
    ISSN: 1600-5759
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...