Purification, amino acid sequence and immunological characterization of Ole e 6, a cysteine‐enriched allergen from olive tree pollen

FEBS Letters

Rodrı́guez, Rosalı́a¹  Villalba, Mayte¹  Batanero, Eva¹  Ledesma, Amalia¹ 

[1] Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Quı́mica, Universidad Complutense, 28040 Madrid, Spain

关键词: Allergen;    Olive pollen;    Ole e 6;    Amino acid sequence;   

DOI  :  10.1016/S0014-5793(97)00582-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (pI 4.2) polypeptide chain protein. Its NH₂-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 NH₂-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-X₃-Cys-X₃-Cys are present. No sequence similarity has been found between this protein and other previously described polypeptides.

【 授权许可】

Unknown