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  • 1
    Electronic Resource
    Electronic Resource
    Laboratory diagnosis of toxigenic Clostridium difficile by polymerase chain reaction: presence of toxin genes and their stable expression in toxigenic isolates from Japanese individuals (1999)
    Springer
    Journal of gastroenterology 34 (1999), S. 41-45 
    Details
    ISSN: 1435-5922
    Keywords: Key words:Clostridium difficile ; PCR ; cytotoxicity ; definitive diagnosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Clostridium difficile causes pseudomembranous colitis and antibiotic-associated diarrhea. The definitive diagnosis of C. difficile infection is finally accomplished by the isolation of toxigenic C. difficile. However, only a small number of Japanese clinical laboratories are able to reach a definitive diagnosis of C. difficile infection, probably because simple reliable assays for toxins in the isolates are not available. In this study, we examined the compatibility of a polymerase chain reaction (PCR) assay and tissue culture assay to identify toxigenic C. difficile, in toxigenic and nontoxigenic C. difficile isolates from Japanese patients and healthy carriers. The specificity of PCR primers was demonstrated by restriction endonuclease digestion and seminested PCR in C. difficile VPI 10463 strain. No PCR product was amplified in the eight other clostridial species used to check the specifiecty of the PCR assay. The detection limit was 103 cells. Both toxin A and toxin B genes (the genes encoding the major virulence factors of C. difficile) were detected in 58 toxigenic C. difficile isolates, which showed a wide range of cytotoxic activity in tissue culture assays. Neither of the toxin genes was carried by 40 nontoxigenic strains of C. difficile. The results of this study strongly suggest that a definitive diagnosis of C. difficile infection can be accomplished by PCR detection of the toxin genes rather than by tissue culture assay of isolates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s005350050214
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  • 2
    Electronic Resource
    Electronic Resource
    Iodide sensitive sensor based on a supported bilayer lipid membrane containing a cluster form of carbon (fullerene C60) (1996)
    Weinheim : Wiley-Blackwell
    Electroanalysis 8 (1996), S. 1020-1022 
    Details
    ISSN: 1040-0397
    Keywords: Iodide ; Bilayer lipid membrane ; C60 ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The iodide ion sensitivity of a solid-supported bilayer lipid membrane (s-BLM) containing buckminsterfullerene(C60) as an electron mediator has been investigated using the cyclic voltammetry technique. We have shown that C60 in a lipid bilayer environment produces a unique and simple system for the detection of iodide. The sensitivity of C60-containing s-BLM to I- is excellent with a linear response in the range from 10-8 to 10-2 M. The use of fullerene C60-doped s-BLMs as sensors and devices for detecting other species is proposed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elan.1140081108
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Large scale purification of myo-inositol monophosphate phosphatase from porcine brains (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 542-546 
    Details
    ISSN: 0006-3592
    Keywords: purification ; inositol monophosphatase ; lithium ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: myo-Inositol monophosphate phosphatase (IMPase) has been purified 888-fold to apparent homogeneity from procine brains. The purification procedure involves: homogenization, ammonium sulfate fractionation, and a number of ion-exchange and gel-filtration chromatography steps. The purified enzyme exhibited a final specific activity of 932 nmol · min-1 · mg-1. The molecular mass of the enzyme was estimated to be 29kDa by SDS poly-acrylamide gel electrophoresis and 58 ± 5 kDa by HPLC gel filtration in 10mM Tris-HCI, pH 7.4. Kinetic measurements have shown that the apparent Km value of the phosphatase for the utilization of inositol-1-phosphate and β-glycerol phosphate are 3.20 × 10-4 and 8 × 10-3 M, respectively. Similar to the same enzyme isolated from bovine brains, the porcine brain enzyme has been shown to be inhibited by lithium. The K1 was determined to be 6.38 × 10-4 M and the inhibition is uncompetitive. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260480517
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