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  • 1995-1999  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 25 (1995), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Candida albicans enolase is one of the important allergens in Candida allergy. We isolated and purified 46 kDa C. albicans enolase (CAE) from C. albicans and characterized epitopes for IgE antibody by lectin-blotting and enzymatic digestion followed by sodium dodecyl sulfale polyacrylamide gel electrophoresis (SDS-PAGE) and immunobiotting. Lectin blotting and deglycozilation indicated that this protein did not contain polysaccharide side chains. The purified CAE and recombinant fusion protein produced from CAE gene possessed common epitopes for IgE antibody. We estimated IgE binding epitopes on the basis of reported amino acid sequences from the analysis of cDNA encoding CAE. V8 protease digestion of CAE gave six polypeptide fragments (A-F). The N-termini of each fragment were confirmed by amino acid sequence and the C-termini were estimated by molecular weights of each fragment and the specific cutting site of V8 protease. Fragment C (25.0 kDa; F-171-I-399) reacted to 90% IgE antibodies examined, whereas fragments D (21.0 kDa; F-171-1-360), E (16.2kDa: F-171-D-317) and F (13.0kDa; A-47-E-170) showed no IgE binding. Our results suggest that epitopes for IgE antibodies exist near the C-terminal of the protein.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 27 (1997), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Candida albicans crossreacts with Saccharomyces cerevisiae or Pityrosporum ovate at the IgE level. However, the extent of crossreactivity of C. alhicans with other yeast species is not known.Objective The crossreactivity at the immunoglobulin E (IgE) level of Candida alhicans with other pathogenic Candida species and to the airborne yeast species Cryptococcus and Rhodotorula was studied by immunoblot analysis.Methods Crude antigens, designated as heat extract, were prepared from 13 different yeast species and a dot blot test was performed to detect IgE antibodies against each of the heat extracts in 349 patients with allergies who were positive for IgE antibodies against C alhicans in a CAP system.Results In the dot blot test, most of the sera reacted with the heat extracts of not only C. albicans but also those prepared from the other yeast species. The sera of 41 of the 349 patients (11.7%) reacted with the heat extracts of all 13 yeast species. The extent of the binding of IgE antibodies to multiple yeast species correlated with both the fluorescence intensities measured in the CAP system and the intensities of dots generated by the heat extract of C. alhicans in the dot blot test. In an inhibition dot blot test, mannoproteins. but not proteins, of C. albicans strongly inhibited the subsequent binding of IgE antibodies to all yeast species.Conclusion Our data suggest that the C. albicans mannoproteins are responsible for the crossreactivity among these yeast species at the IgE level.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 25 (1995), S. 0 
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Candida albicans 46 kDa protein, a glycolytic enolase enzyme, is an important allergen of the yeast. The purpose of the study was to detect circulating IgE and IgG antibodies against C. albicans enolase (CAE). We isolated CAE using sequential DEAE Sephacel and Pl 1 column chromatography from spheroptasts of C. albicans, and delected IgE and IgG antibody against CAE by immunoblotting. Crossreactivity of enolose of C. albicans and Saccharomyces cerevisiae was also examined by immunoblotting and immunoblot inhibition test. Among 54 sera with positive IgE RAST to C. albicans, IgE antibody against CAE was detected in 20 sera (37%) and IgG antibody in 27 sera (50%). The allergenic potency of CAE was confirmed using a skin-prick test in three patients. Simultaneous IgE binding to S. cerevisiae enolase was only observed in four out of 20 sera reacting to CAE. Pre-treatment of sera with CAE completely inhibited IgE binding to S. cerevisiae enolase. Whereas the latter only partially inhibited IgE binding to CAE. These results suggest that CAE shares some crossreacting epitopes with S. cerevisiae enolase, representing minor components of CAE but dominant segments of S. cerevisiae enolase.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Artificial life and robotics 3 (1999), S. 106-111 
    ISSN: 1614-7456
    Keywords: Evolutionary robotics ; Developmental process ; Nontrivial behaviors ; Canalization ; Walking robot
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science
    Notes: Abstract Recently, evolutionary robotics (ER) has been attracting a lot of attention in the field of robotics artificial life and so on. ER approaches are expected to provide feasible methods to design controllers for autonomous mobile robots with less human intervention. However, most of the conventional studies in ER have been aiming at obtaining very simple (trivial) behaviors such as obstacle avoiding, wall following, and target approaching. To make the ER approach more fruitful, we should pay close attention to obtaining nontrivial behaviors. Based on these considerations, in this paper we propose a method for obtaining nontrivial behaviors using a developmental process with a carefully arranged grafting method. To verify the validity, we apply our idea to the construction of neural controllers that can cope with rough terrain.
    Type of Medium: Electronic Resource
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