hevein


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hevein

(hē′vē-ĭn)
A protein allergen found in natural rubber latex that stimulates neutrophils to release oxygen radicals. Hevein is a lectin responsible for the IgE-mediated hypersensitivity response to latex products.
References in periodicals archive ?
Lectins have been classified into 12 different families based on their domain structures and phylogenetic analyses: ABA (Agaricus bisporus agglutinin), amaranthin, chitinase-related agglutinin (CRA), cyanovirin, Euonymus europaeus agglutinin (EEA), Galanthus nivalis agglutinin (GNA), hevein, jacalins, legume lectin, lysin motif (LysM), and nictaba and ricin B families (Jiang et al.
After leaving Apocalyptica in early 2000s, it seems Max unveiled his full potential - besides being a cellist in Finnish National Opera Orchestra, he became member of a multi genre metal band Hevein and a Finnish folk-pop band Tekija Tuntematon, whose music is based on Finnish poetry.
4] Thirteen different hevein latex proteins have been recognised as allergens by the Allergen Nomenclature Subcommittee of the World Health Organization/International Union of Immunological Societies.
Latex allergenicity has been determined by measuring the levels of the clinically relevant hevein allergens (Hev b 1, Hev b 3, Hev b 5 and Hev b 6.
Demonstration by mass spectrometry that pseudo-hevien and hevein have ragged C-terminal sequences.
IgE epitope analysis of the hevein preprotein; a major latex allergen.
A recently identified 46/110-kd protein, is common among health care workers,[40] as is the hevein preprotein.
Of note, plant lectins can be divided into 12 different families, including ABA (Agaricus bisporus agglutinin), Amaranthin, CRA (chitinase-related agglutinin), Cyanovirin, EEA (Euonymus europaeus agglutinin), GNA (Galanthus nivalis agglutinin), Hevein, Jacalins, Legume lectin, LysM (lysin motif), Nictaba and Ricin_B families (Van Damme et al.
Four major lectin families, namely, the legume lectins, the chitin-binding lectins composed of hevein domains, the type2 ribosome-inactivating proteins and the monocot mannose-binding lectins comprise the majority of all currently known plant lectins (Van Damme et al.