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cynodon nlemfuensis/hipersensitivitas

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Epidemiological and experimental studies suggest that air pollution has a negative impact on human health and modifies the environment. However, the clinical implications of changes in environmental allergens secondary to air pollution have been little
BACKGROUND Profilin, an actin-binding protein, was previously described as a panallergen which is involved in about 20% of the crossreactivity found among pollen and food allergic patients. This allergen is usually under-represented in natural extracts used for allergy diagnosis. OBJECTIVE To obtain

Identification of Bermuda grass (Cynodon dactylon)--pollen allergens by electroblotting.

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Bermuda grass-pollen proteins were electrophoretically separated on polyacrylamide gels and transferred to nitrocellulose where IgE-binding components were detected by reaction with individual patient's serum and 125I-labeled antihuman IgE. Seventeen pollen components (in the molecular weight (MW)

Identification of allergens and antigens of Bermuda grass (Cynodon dactylon) pollen by immunoblot analysis.

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Allergens and antigens of Bermuda grass pollen fractionated by SDS-polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes were identified using twenty-one sera of Bermuda grass pollen-allergic patients. The IgE- and IgG-binding pollen components transferred to nitrocellulose
BACKGROUND Bermuda grass pollen (BGP) is an increasingly important seasonal aeroallergen in Australia and other subtropical and temperate regions. BGP shares minimal allergenic cross-reactivity with pollens of rye grass or other Pooideae grasses often used for desensitization regimens in grass

A species-specific monoclonal antibody to Cynodon dactylon.

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BACKGROUND It is usually difficult to differentiate between the pollens of different grass species on the basis of their appearance under a microscope, as they often appear similar. Such distinctions are important when interpreting the clinical relevance of pollens in air samples as individuals can

Characterization of the isoforms of the group I allergen of Cynodon dactylon.

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BACKGROUND The group I allergen of Cynodon dactylon, Cyn d I, was found to consist of four to 10 isoforms. METHODS We studied the isoforms with the use of two-dimensional gel electrophoresis. The antigenic difference of the isoforms was evaluated by radioimmunoprecipitation with monoclonal

Relevance of Allergenic Sensitization to Cynodon dactylon and Phragmites communis: Cross-reactivity With Pooideae Grasses.

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The homologous group of sweet grasses belongs to the Pooideae subfamily, but grass pollen species from other subfamilies can also cause allergy, such as Cynodon dactylon (Chloridoideae) and Phragmites communis (Arundinoideae). C dactylon and P communis have not been included in the sweet grasses

An immunoelectrophoretic analysis of the allergens of Cynodon dactylon (Bermuda grass) pollen.

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A crude extract of Cynodon dactylon (Bermuda grass) pollen was obtained by extraction, centrifugation, dialysis, and lyophilization. The corresponding polyspecific rabbit antibodies were obtained by immunization, bleeding, and purification and were used for a cross immunoelectrophoretic analysis of
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