Natural and recombinant enzymatically active or inactive bee venom phospholipase A 2 has the same potency to release histamine from basophils in patients with Hymenoptera allergy

The Journal of Allergy and Clinical Immunology

Volumn 95, Issue 6, 1995, Pages 1229-1235

  Förster, Elisabeth ^a   Dudlerb, Thomas ^a   Gmachl, Michael ^a   Aberer, Werner ^a   Urbanek, Radvan ^a   Suter, Mark ^a  

^a Vienna Austria Davos Platz Switzerland and Salzburg Austria ^*

Author keywords

bee venom phospholipase A 2; glycosylation; Histamine release; recombinant allergen

Indexed keywords

BEE VENOM; HISTAMINE; IMMUNOGLOBULIN E; PHOSPHOLIPASE A2; RECOMBINANT PROTEIN;

ALLERGENICITY; AMINO ACID SUBSTITUTION; ARTICLE; BASOPHIL; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; HISTAMINE RELEASE; HUMAN; HUMAN CELL; HYMENOPTERA; INSECT ALLERGY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING;

BEE VENOMS; COMPARATIVE STUDY; HISTAMINE RELEASE; HUMAN; HYPERSENSITIVITY; PHOSPHOLIPASES A; POINT MUTATION; RECOMBINANT PROTEINS; SUPPORT, NON-U.S. GOV'T;

EID: 0029063616     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0091-6749(95)70080-3     Document Type: Article

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