These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: [Adherence of Candida albicans to acrylic surfaces].
    Author: Kaita H.
    Journal: Fukuoka Shika Daigaku Gakkai Zasshi; 1989; 16(3):407-22. PubMed ID: 2486701.
    Abstract:
    The ability of Candida albicans IFO 1385 to adhere to acrylic and the partial characterization of an adhesive substance, named AS, which was isolated from the yeast, were studied in vitro. The results obtained were as follows: 1. The cells cultured in the synthetic media (YNB) containing 500 mM galactose showed a much greater tendency to adhere than did those cells cultured in the YNB containing 500 mM glucose. 2. More cells prepared by the standing cultivation adhered to acrylic than did those prepared by the stirring cultivation. 3. A large number of the adherent cells was obtained when the acrylic plates were incubated at 37 degrees C for 90 min in the cell suspension at a concentration of 1.0 x 10(7) cells/ml. The plates were observed without staining. 4. AS was isolated from the surface of C. albicans, grown on different carbon sources (50 mM glucose, 500 mM glucose and 500 mM galactose), by treatment with ultrasonication. 5. Three different kinds of AS isolated from the three carbon sources were slightly soluble in distilled water. All were similar in composition to each other, and contained 62-68% carbohydrate (as glucose) and 23-26% protein (as BSA). 6. Silica particles adhered to acrylic coated with AS and pretreatment of acrylic with AS promoted C. albicans adhesion. However, similar pretreatment inhibited subsequent Candida glabrata and Candida krusei adhesion. As to subsequent adhesion of Candida tropicalis, no significant data were obtained. 7. Adhesion assay using the silica particles, the adhesive ability of the AS was significantly reduced by treatment with trypsin or pronase E, but not with papain, alpha-amylase, dextranase or zymolyase.
    [Abstract] [Full Text] [Related] [New Search]