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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Pediatric allergy and immunology 7 (1996), S. 0 
    ISSN: 1399-3038
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Previous studies have found that questions are considerably less sensitive for predicting sensitization to dust mites than to pollens or to household pets. We studied 1160 children with respiratory symptoms to find whether the sensitivity for predicting mite allergy could be increased by asking several rather than single questions. Parents accompanying the children were asked standardized validated questions. Of the four individual questions relevant to mites, the one with the highest sensitivity for predicting a positive skin prick test to this allergen was whether the symptoms were worse when the house was heing swept, vacuumed or dusted (29. 8%). If an affirmative answer to that question, or to any of the other three questions, was taken as predictive of sensitization, the sensitivity increased to 54. 2%. However, requiring only a single affirmative answer to this combination of questions decreased the specificity. The sensitivity of the combination of questions was comparable to that of questions for predicting positive tests to tree pollens (56. 4%), cats (56. 4%), grass pollens (52. 5%) and dogs (51. 4%). We conclude that asking a combination of questions is as useful for indicating possible sensitization to dust mite as are questions for detecting sensitization to other common inhalant allergens.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 191 (1996), S. 164-171 
    ISSN: 1615-6102
    Keywords: Calcium binding proteins ; Calreticulin ; Endoplasmic reticulum ; Plants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the present study we have investigated the presence and distribution of calreticulin in plant protoplasts. Calreticulin was purified from plant homogenates using a selective ammonium sulfate precipitation procedure developed for the purification of mammalian calreticulins and shown to bind calcium in45Ca2+ overlay assays. The protein was localized to plant cell endoplasmic reticulum by the indirect immunofluorescence staining of protoplasts with anti-calreticulin antibodies. No calreticulin was observed within large vacuoles. We conclude that calreticulin is present in the endoplasmic reticulum of plant cells, where, by analogy to the mammalian endoplasmic reticulum, it may play a major role in Ca2+ binding and storage.
    Type of Medium: Electronic Resource
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