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Archives of pharmacal research

The identification of surface interaction of apotransferrin with Candida albicans.


PMID 24263410

Abstract

Our recent data indicate that apotransferrin, an iron-chelating protein, has anti-candidal activity by binding to the Candida albicans surface rather than just simple iron-chelation. Following that study, in this present study, we investigated the nature of the candidal surface substance that is responsible for the anticandidal activity by using (59)Fe(3+)-apotransferrin and biological assay methods. Data resulting from the binding studies showed that the yeast cells had one class of binding sites as analyzed by the Scatchard equation, and the binding was specific as determined by competitive binding assay with unlabeled and labeled transferrin. All these observations indicate that there is a substance(s) that mediates the binding. Thus, a mannoprotein-like substance was extracted from C. albicans surface using hot water-treatment. Radioisotope binding study revealed that the substance blocked the transferrin binding. At 25xa0μg of IHS (inhibitory substance) addition, there was 65xa0% inhibition of the transferrin binding to C. albicans (5xa0×xa010(7)xa0cells/ml) (Pxa0

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