Characterization of Dac g 4, a major basic allergen from Dactylis glomerata pollen.
J Allergy Clin Immunol
; 98(6 Pt 1): 1065-72, 1996 Dec.
Article
in En
| MEDLINE
| ID: mdl-8977507
ABSTRACT
Monoclonal antibodies were produced against Dac g 4, a purified major basic allergen from Dactylis glomerata pollen. Their ability to be used for immunopurification of Dac g 4 was studied on a BIAcore apparatus (Pharmacia). The allergen was purified by affinity chromatography with one monoclonal antibody. Its precise molecular mass, 59,185 +/- 30 d, was determined by mass spectrometry. Its isoelectric point is 10.4. Sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting showed that Dac g 4-related proteins of similar molecular mass were detected in the majority of allergenic grass pollen species. By double-site ELISAs, we have estimated that Dac g 4 represents about 6% of the total proteins from a water-soluble extract. One monoclonal antibody (mAb H) recognized a 60 kd cross-reactive protein in other grass pollens, though none in any of the tree or weed pollens tested. Inhibition studies of IgE antibody binding to Dac g 4 with pollen extracts confirmed the presence of cross-reactive allergens in Secale cereale, Lolium perenne, Festuca elatior, Holcus lanatus, Bromus arvensis, Poa pratense, Hordeum sativum, and Phleum pratense.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Plant Proteins
/
Pollen
/
Allergens
Limits:
Animals
Language:
En
Journal:
J Allergy Clin Immunol
Year:
1996
Document type:
Article
Affiliation country:
France