International Archives of Allergy and Immunology
Allergens, Immunotherapy and Management
Antigenic Analysis (IgE and Monoclonal Antibodies) of the Major Shrimp Allergen Pen a 1 (Tropomyosin) from Penaeus aztecusReese G. · Daul C.B. · Lehrer S.B.Section of Clinical Immunology and Allergy, Tulane University Medical Center, New Orleans, La., USA
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Article / Publication Details
Published online: September 04, 2009
Issue release date: 1995
Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0
ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)
For additional information: https://www.karger.com/IAA
Abstract
Pen a 1, the major shrimp allergen from the brown shrimp Penaeus aztecus was purified by preparative SDS-PAGE. Peptides were generated from Pen a 1 by CNBr cleavage and endoproteinase (Lys-C, Glu-C, trypsin, alkaline protease, Arg-C, chymotrypsin) digestion. The molecular weights of the resulting CNBr cleavage and enzymatic digestion products, separated by peptide SDS-PAGE, ranged from 1.5 to 20 kD. Following SDS-PAGE and semidry blotting, the analysis of monoclonal antibody (mAb) and subjects’ IgE reactivities demonstrated that with the exception of alkaline protease, all cleavage procedures yielded IgE-binding peptides. However, since not all peptides of every digest bind IgE, it appears that IgE-binding epitopes are restricted to certain parts of the Pen a 1 molecule. mAbs bound to CNBr, Lys-C, trypsin, Glu-C and Arg-C peptides. Since mAbs reacted to several peptides from the same digest, Pen a 1 may have several similar epitopes. The comparison of IgE and mAb reactivities demonstrated similar but not identical binding patterns.
© 1995 S. Karger AG, Basel
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Article / Publication Details
Published online: September 04, 2009
Issue release date: 1995
Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0
ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)
For additional information: https://www.karger.com/IAA
Copyright / Drug Dosage / Disclaimer
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