Olive-pollen profilin. Molecular and immunologic properties.
Olive-pollen profilin has been isolated and characterized as a significant allergen. Its molecular properties, such as a molecular mass of 15 kDa; amino-acid composition; and secondary repetitive structure percentages of 15% alpha-helix, 33% beta-strand, 20% beta-turn, and 32% random coil, have been determined. Its allergenic capability, a recognition frequency estimated at 24% of olive-hypersensitive patients, and high cross-reactivity with all the pollen used have been found. The presence of conformation epitopes in the olive profilin, as well as a high structural and immunologic similarity to other pollen sources such as birch and ash, can be established from these studies.
Ledesma
A
A
Depto. Bioquímica y Biología Molecular, Facultad de Química, UCM, Madrid, Spain.
Rodríguez
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R
Villalba
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M
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002942:Circular Dichroism; D003285:Contractile Proteins; D003429:Cross Reactions / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D006801:Humans; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000276:immunology; D008840:Microfilament Proteins / Q000737:chemistry / Q000235:genetics* / Q000276:immunology* / Q000302:isolation & purification; D008970:Molecular Weight; D051304:Profilins
D000596:Amino Acids; D003285:Contractile Proteins; D000939:Epitopes; D008840:Microfilament Proteins; D051304:Profilins; D007073:Immunoglobulin E