We studied total and specific serum IgE levels cross-sectionally, potential predictors of obstructive lung disease, in a stratified random sample of 18-73-year-old adults (n = 1512). The attendance rate was 84%. The total IgE level and prevalences of specific IgE antibodies against house dust mite and cat were higher for men than for women. Specific IgE levels decreased by increasing age, while total IgE decreased in women only. Smokers had a higher IgE level than non-smokers, while non-smokers had more often specific IgE antibodies against timothy and birch than smokers. Subjects with occupational dust or gas exposure had a higher total IgE level than unexposed. The general population prevalences were for specific IgE antibodies against timothy 4.5%, house dust mite 3.2%, birch 2.6%, cat dander 1.6% mould 0.2% and against any of these 7.6%. In a multivariate analysis age, occupational dust or gas exposure as well as the interaction terms between sex and age and between smoking and pack-years were independent predictors for total IgE levels. Male sex, young age, never having smoked and the season of the year were independent predictors for having one or more of the five specific IgE antibodies. Subjects with total serum IgE in the highest quintile (> or = 66 kU/l) had an adjusted odds ratio of 37 (95% confidence interval: 11-120) for having one or more of the specific IgE antibodies examined, compared with those in the lowest quintile (< 5 kU/l). Demographic and environmental factors were thus predictors of total and specific IgE levels in this adult community.(ABSTRACT TRUNCATED AT 250 WORDS)

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The complete primary structure of allergen M of cod (Gadus callarias L.) is presented. The amino acid sequence of fragment TM1, the NH2-terminal peptide of allergen M, was elucidated by the dansyl-Edman method. It consists of 75 amino acids and 1 glucose residue (mol. wt. 8,492). By summation of the sequence data of fragment TM1 and the previously reported fragment TM2, the intact allergen M has 113 residues (mol. wt. 12,328). Fragment TM1 of cod shows less homology (30.6 percent) with the corresponding fragments of other reported fish species than does fragment TM2 (42.1 percent); the intact allergen M shows 34.5 percent homology. The single half cystine of allergen M was shown to be blocked. Gas chromatographic analysis of the reduced and nonreduced allergen M suggested that the glucose is bound to Cys 18 through an S-glucosidic bond.

The major allergen of codfish (Allergen M) is a muscle protein belonging to the family of calcium binding parvalbumins. The primary structure ol the molecule was established and the molecular weight was estimated from the sequence data to be 12,328, Allergen M consists of 113 amino acid residues and one residue of glucose, A molecular arrangement of three domains (AB, CD and EF -the latter two bind one Ca2+ ion each) was described for Allergen M, analogous to carp parvalbumin pi 4,25, The suggested strucutre was based on the extensive intramolecular amino acid homologies and the immunocheinical cross-reactivities of the intact molecule and the two major isolated fragments.The immunological structure of Allergen M was studied by: 1, Modification of certain amino acids residues and study of the reactivity of the modified derivatives, 2, Examination of the immunochemical reactivity of a large number of overlapping peptides obtained by limited and selective tryptic hydrolyses, 3, Solid phase peptide synthesis (SPPS) of segments selected in regard to the reactivity of pre-examined native peptides.The immunological reactivity of the derivatives of Allergen M was assigned by: I, Rocket line immunoelectrophoresis and quantitative precipitation using rabbit anti-Allergen M in precipitating antibody-mediated reactions and, 2, RAST/RAST-inhibition and PK test/PKtest inhibition using sera from individuals allergic to codfish in igE-mediated reactions.The modification of Tyr-30 and Arg-75 in isolated and purified peptides indicated that the former was part of a reactive site whereas the latter did not contribute to the activity. Masking of Arg-residue or unchelating the two calcium ions from the native Allergen M, with the resulting perturbation of the tertiary structure, decreased the allergenicity by approximately 25 %.Two major fragments of Allergen M were produced and purified; TM 1 (residues 1-75) comprising domains AB and CD, and TM2 (residues 76-113) covering domain EF, Both were immunologically reactive; TM 1 showing intermediate reactivity between Allergen M and TM2, A high degree of immunological cross reactivity was evident between TM 1 and TM2, The finding was in concert with the high intramolecular amino acid homologies of Allergen M, and suggested that the reactive sites were repetitively distributed along the polypeptide chain.The immunological reactivity of several long-sequence overlapping peptides obtained by limited and selective trypsin hydrolysis of Allergen M was studied. The immunologically reactive sites were accordingly assigned to the following regions of the chain: 1, Residues 33^4 on the junction between the AB and CD domains, 2, Residues 65-74 on the corresponding junction between the CD and EF domains, 3, Residues 88-96 on the calcium binding loop of the EF domain.These results were cross-examined by SPPS of these segments, A synthetic peptide with the sequence 49-64 of Allergen M, located in the calcium binding loop of the CD domain confirmed the immunological reactivity of this region, Peptide...

Allergy to fish is common in Northern Europe. Variable reactions to different fish species are usually experienced among fish allergic patients. The allergens of cod fish and particularly the major allergen parvalbumin beta (Gadus callarias) have been extensively studied in Norway. In the present communication, the white muscle parvalbumin was similarly found to be a major allergen in Atlantic salmon (Salmo salar, Sal sl). A purified salmon parvalbumin was obtained by anion exchange chromatography, gel filtration chromatography (GFC) and high-performance liquid chromatography (HPLC) of the muscle extracts. The antigenicity and allergenicity of salmon parvalbumin were confirmed using various immunologic and electrophoretic techniques. The protein is representative for several isoallergens judged by the amino acid (AA) sequence variance at certain sites in the AA sequence of CNBr cleavage peptides. Using sera from patients with cod and salmon allergy Sal sl was demonstrated to be the major allergen of Atlantic salmon, as judged by RAST- and ELISA-inhibitions and crossed radioimmunoelectrophoresis (CRIE) techniques. The protein was also demonstrated to be antigenic by the use of polyclonal cod and salmon antibodies in IgG ELISA and immunoelectrophoretic methods. Cloning of parvalbumin cDNA from Atlantic salmon was performed based on an alignment of parvalbumin AA sequences from other species. A probe was generated by PCR and used for screening a salmon muscle cDNA-library. Subcloning and sequencing of two hybridizing clones revealed transcripts from two different parvalbumin genes. The translated sequences of both clones belong to the beta-lineage of parvalbumins and include the entire coding region.