Crystallization and preliminary diffraction data of a major pollen allergen. Crystal growth separates a low molecular weight form with elevated biological activity.

Bufe, A; Betzel, C; Schramm, G; Petersen, A; Becker, W M; Schlaak, M; Perbandt, M; Dauter, Z; Weber, W

Bufe, A; Betzel, C; Schramm, G; Petersen, A; Becker, W M; Schlaak, M; Perbandt, M; Dauter, Z; Weber, W.

Affiliation

Bufe A; Laborgruppe Allergologie, Forschungszentrum Borstel, Parkallee 22, D-23845 Borstel, Germany.

J Biol Chem ; 271(44): 27193-6, 1996 Nov 01.

Article in En | MEDLINE | ID: mdl-8910284

Subject(s)

Allergens/chemistry; Plant Proteins/chemistry; Pollen; Ribonucleases/chemistry; Amino Acid Sequence; Asthma/etiology; Crystallization; Crystallography, X-Ray; Escherichia coli; Humans; Immunoblotting; Molecular Sequence Data; Molecular Weight; Peptide Fragments/chemistry; Plant Proteins/isolation & purification; Poaceae; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Rhinitis, Allergic, Seasonal/etiology; Ribonucleases/isolation & purification; Ribonucleases/metabolism

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Database: MEDLINE Main subject: Plant Proteins / Pollen / Ribonucleases / Allergens Type of study: Etiology_studies Language: En Journal: J Biol Chem Year: 1996 Type: Article Affiliation country: Germany

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