A component of Alternaria extract, previously identified as the major allergen, Alt a I1563, was purified to homogeneity from Alternaria mycelium by means of acetone precipitation and ion-exchange chromatography. The homogeneity of Alt a I1563 was assessed by one single band after sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by one single radiolabeled band after transfer to nitrocellulose, and by one single peak after size-exclusion chromatography by high-performance liquid chromatography. Alt a I1563 was isolated as a heat-stable acidic glycoprotein (carbohydrate content, 20%; pI, 4.0 to 4.5; 31 kd). The role of the carbohydrate moiety in the allergenicity is suggested. This major allergen is located in the cytoplasm of mycelium and spore.
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http://dx.doi.org/10.1016/0091-6749(91)90247-l | DOI Listing |
J Allergy Clin Immunol
December 1991
Unité de Mycologie, Institut Pasteur, Paris, France.
A component of Alternaria extract, previously identified as the major allergen, Alt a I1563, was purified to homogeneity from Alternaria mycelium by means of acetone precipitation and ion-exchange chromatography. The homogeneity of Alt a I1563 was assessed by one single band after sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by one single radiolabeled band after transfer to nitrocellulose, and by one single peak after size-exclusion chromatography by high-performance liquid chromatography. Alt a I1563 was isolated as a heat-stable acidic glycoprotein (carbohydrate content, 20%; pI, 4.
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