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Purification, amino acid sequence and immunological characterization of Ole e 6, a cysteine‐enriched allergen from olive tree pollen
Author(s) -
Batanero Eva,
Ledesma Amalia,
Villalba Mayte,
Rodrı́guez Rosalı́a
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00582-6
Subject(s) - allergen , cysteine , pollen , peptide sequence , biochemistry , chemistry , amino acid , sequence (biology) , biology , botany , gene , allergy , immunology , enzyme
The Ole e 6 allergen from olive tree pollen has been isolated by combining gel permeation and reverse‐phase chromatographies. It is a single and highly acidic (p I 4.2) polypeptide chain protein. Its NH 2 ‐terminal amino acid sequence has been determined by Edman degradation. Total RNA from the olive tree pollen was isolated, and a specific cDNA was amplified by the polymerase chain reaction using a degenerate oligonucleotide primer designed according to the NH 2 ‐terminal sequence of the protein. The nucleotide sequencing of the cDNA rendered an open reading frame encoding a 50 amino acid polypeptide chain, in which two sets of the sequential motif Cys‐X 3 ‐Cys‐X 3 ‐Cys are present. No sequence similarity has been found between this protein and other previously described polypeptides.