Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.
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Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat. / Suhr, Martin; Wicklein, Daniel; Lepp, Ute; Becker, Wolf-Meinhard.
in: MOL NUTR FOOD RES, Jahrgang 48, Nr. 5, 5, 2004, S. 390-399.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.
AU - Suhr, Martin
AU - Wicklein, Daniel
AU - Lepp, Ute
AU - Becker, Wolf-Meinhard
PY - 2004
Y1 - 2004
N2 - Peanut allergy is a significant health problem because of its prevalence and the potential severity of the allergic reaction. The characterization of peanut allergens is crucial to the understanding of the mechanism of peanut allergy. Recently, we described cloning of the peanut allergen Ara h 6. The aim of this study was isolation and further characterization of nAra h 6. We purified nAra h 6 from crude peanut extract using gel filtration and anion exchange chromatography. The preparation was further characterized by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) with subsequent immunoblotting. Stability of nAra h 6 was studied by an in vitro digestibility assay as well as by resistance against thermal processing. Sequencing of nAra h 6 identified the N-terminal amino acid sequence as MRRERGRQGDSSS. Further results clearly demonstrated stability of nAra h 6 against pepsin digestion and heating. Immunoglobulin G (IgE) binding analysis and its biological activity shown by RBL 25/30-test of natural Ara h 6 supported the importance of this peanut allergen. Investigation of nAra h 6 revealed evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.
AB - Peanut allergy is a significant health problem because of its prevalence and the potential severity of the allergic reaction. The characterization of peanut allergens is crucial to the understanding of the mechanism of peanut allergy. Recently, we described cloning of the peanut allergen Ara h 6. The aim of this study was isolation and further characterization of nAra h 6. We purified nAra h 6 from crude peanut extract using gel filtration and anion exchange chromatography. The preparation was further characterized by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) with subsequent immunoblotting. Stability of nAra h 6 was studied by an in vitro digestibility assay as well as by resistance against thermal processing. Sequencing of nAra h 6 identified the N-terminal amino acid sequence as MRRERGRQGDSSS. Further results clearly demonstrated stability of nAra h 6 against pepsin digestion and heating. Immunoglobulin G (IgE) binding analysis and its biological activity shown by RBL 25/30-test of natural Ara h 6 supported the importance of this peanut allergen. Investigation of nAra h 6 revealed evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat.
KW - Humans
KW - Immunoblotting
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Electrophoresis, Gel, Two-Dimensional
KW - Chromatography, Gel
KW - 2S Albumins, Plant
KW - Allergens/chemistry/isolation & purification/metabolism
KW - Antigens, Plant
KW - Chromatography, Ion Exchange
KW - Drug Stability
KW - Hot Temperature
KW - Immunoglobulin E/immunology
KW - Peanut Hypersensitivity/immunology
KW - Pepsin A/metabolism
KW - Peptide Fragments/chemistry/immunology/metabolism
KW - Humans
KW - Immunoblotting
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Electrophoresis, Gel, Two-Dimensional
KW - Chromatography, Gel
KW - 2S Albumins, Plant
KW - Allergens/chemistry/isolation & purification/metabolism
KW - Antigens, Plant
KW - Chromatography, Ion Exchange
KW - Drug Stability
KW - Hot Temperature
KW - Immunoglobulin E/immunology
KW - Peanut Hypersensitivity/immunology
KW - Pepsin A/metabolism
KW - Peptide Fragments/chemistry/immunology/metabolism
M3 - SCORING: Journal article
VL - 48
SP - 390
EP - 399
JO - MOL NUTR FOOD RES
JF - MOL NUTR FOOD RES
SN - 1613-4125
IS - 5
M1 - 5
ER -
