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  • 1
    ISSN: 1432-069X
    Keywords: Candida albicans ; Extracellular proteinase ; Medium pH
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Candida albicans produces a major extracellular proteinase whose activities are observed only in weakly acidic pH. However, in affected lesions, a variety of pH conditions exist, including neutral pH. To verify the pathological importance of the extracellular proteinase, the correlation between culture medium pH, extracellular proteinase activity, and cell growth of C. albicans was followed for 3 weeks with unbuffered and insoluble stratum corneum-supplemented liquid media. Each medium pH, initially adjusted within a range of pH 3–7 by the addition of sodium hydroxide or hydrochloric acid solution, was acidified, and a subsequent high proteolytic activity and rapid fungal growth were observed. After full fungal growth, neutralization of each medium to pH 7 and reduction of proteinase activity occurred. Results from a glucose addition experiment suggest that acidification of each medium was produced by the acid formation from glucose and neutralization by the exhaustion of glucose and increase of ammonia from denatured stratum corneum. These data suggest that extracellular proteinase from C. albicans could act as a virulence factor under a wide range of pH conditions by the acidification of the environmental pH close to the organism.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 281 (1989), S. 78-80 
    ISSN: 1432-069X
    Keywords: Extracellular proteinase ; Nocardiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1569-8041
    Keywords: DPD ; 5-fluorouracil ; immunohistochemistry ; RT–PCR ; Western blotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background: Dihydropyrimidine dehydrogenase (DPD) is the firstenzyme that metabolizes 5-fluorouracil (5-FU). Until now, enzymatic activityor mRNA expression of DPD has been investigated. However, there are no paperson immunohistochemical evaluation of DPD. We investigated DPD staining onimmunohistochemistry, and examined the relationship among immunohistochemicalscore, protein level and mRNA expression of DPD. Materials and methods: Forty-seven resected colon cancerspecimens, four colon cancer cell lines, two xenografts by colon cancer celllines, and human mononuclear cells were used. Immunohistochemistry wasperformed using DPD monoclonal antibody. Protein levels were determined byWestern blot analysis. And mRNA levels were calculated by semi-quantitativereverse transcription polymerase chain reaction (RT–PCR). Results: DPD was strongly expressed in the cytoplasm of cancercells, and in the cytoplasm of macrophage and plasma cells. Theimmunohistochemical score was more correlated with protein levels (P= 0.0054) than mRNA expression (P = 0.9028). Conclusions: We investigated the characterization of DPDimmunohistochemically, and showed that immunohistochemical expression of DPDcan be used to predict the sensitivity of colorectal carcinomas to 5-FU.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0878
    Keywords: Pituitary ; Pars distalis ; Growth hormone ; Prolactin ; Hormonal specificity ; Immunocytochemistry ; Immunoblot technique ; Amphibians (Urodela, Anura)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract An antiserum was prepared against the recently purified bullfrog (bf) growth hormone (GH); it was applied to sections of brain and pituitary of three urodele (Ambystoma, Pleurodeles and Cynops) and three anuran (Xenopus, Bufo vulgaris and B. japonicus) species. No immunostaining was obtained in the urodele pituitary, being consistent with the results of immunoblot analysis of the pituitary homogenate. In the three anuran species, strong immunoreactivity was observed in GH cells that were concentrated in the posterodorsal region of the pars distalis. No GH-like immunoreactivity was detectable in the brain of any of the species. A comparison using adjacent sections stained with anti-bf prolactin (PRL) confirmed the anteroventral localization of PRL cells. Colocalization of GH and PRL was not apparent. These data suggest that the molecular structure of amphibian GHs is considerably different between anurans and urodeles. The antiserum used in the present work shows a high species specificity, recognizing only anuran GHs. In contrast anti-bfPRLlabeled PRL cells in all the amphibian species studied in the present work, suggesting that PRLs possess common amino acid sequences recognized by the anti-bfPRL.
    Type of Medium: Electronic Resource
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