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Table of Contents
Vol. 109, No. 2, 1996
Issue release date: 1996
Section title: Original Paper
Int Arch Allergy Immunol 1996;109:141–149
(DOI:10.1159/000237213)

Characterization of Major Allergens of Parietaria officinalis

Kahlert H.a · Weber B.a · Teppke M.b · Wahl R.a · Cromwell O.a · Fiebig H.a
aAllergopharma Joachim Ganzer KG, Reinbek and bDepartment of Biochemistry and Molecular Biology, University Hamburg, Germany

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: February 07, 1995
Accepted: August 22, 1995
Published online: September 04, 2009
Issue release date: 1996

Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA

Abstract

The major allergens of Parietaria officinalis were characterized with a panel of nine monoclonal antibodies (mAbs). The binding of mAbs and patients’ IgE in Western blots revealed two proteins with similar molecular weights in the range of 8-10 kD. Analysis of the mAb-binding patterns in Western blots of P. officinalis extract under reducing and nonreducing conditions allows the mAbs to be divided into three different groups. mAbs of group I recognize the higher-molecular-weight component (9.4 kD), mAbs of group II recognize the lower component (8.8 kD) and mAbs of group III recognize both proteins. A comparable mAb-binding pattern was observed with Western blots of Parietaria judaica. The mAbs were used for affinity purification of the corresponding proteins from a P. officinalis extract. The purified proteins obtained with mAbs of group I–III inhibit the binding of patients’ IgE (serum pool) to a high degree, indicating that they possess the major IgE-reactive epitopes. The affinity-purified proteins were subjected to SDS-PAGE, blotted and immunologically stained by mAb binding. The results confirmed those obtained with the complete extracts. The N-terminal amino acid sequences of the blotted proteins were analyzed. The sequences of all the proteins contained highly conserved regions: GGVV (positions 4–7) and MPPLL (positions 11–15), alternating with highly variable regions (positions 1–3 for group II and 8–10 for group I). A specific group I sequence appears to be at position 1–3 with the amino acids APA and a specific group II sequence appears to be at position 8–10 with the amino acids GAL. It is possible that the two similar proteins are isoforms of Par·1.

© 1996 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: February 07, 1995
Accepted: August 22, 1995
Published online: September 04, 2009
Issue release date: 1996

Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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