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Biomedical subjects

D Barber

Publications and source records attributed to D Barber.

At least 91 records · Page 5Linked to original sources

Evaluation of immune complexes after immunotherapy with wheat flour in bakers' asthma.

Inhalant food allergy has been described many times in literature, but double-blind clinical trials to support successful hyposensitization to these allergens has seldom been reported. Some authors have suspected that certain adverse reactions after immunotherapy may be mediated by immune complexes. Furthermore, the FDA does not recommend injection therapy with food extracts. We present a study on the detection of adverse effects after immunotherapy with an inhalant food (wheat flour) in a double-blind clinical trial in 26 patients with bakers' asthma. We investigated the presence of circulating immune complexes (CICs) after 2 years of treatment with hyposensitization to wheat flour.

Antigen-Antibody Complex↗

Sensitization to the storage mite Lepidoglyphus destructor in wheat flour respiratory allergy.

Occupational allergy due to hypersensitivity to cereal flours is relatively common among bakers and grain-store workers. Storage mites can contaminate wheat flour and could be an important cause of allergic symptoms due to inhalation. Forty-three patients with criteria for allergic sensitization to wheat flour (skin tests, specific IgE to wheat flour and positive challenge tests) were included in a study to investigate the prevalence of cosensitization to Lepidoglyphus destructor (Ld). This mite was the predominant species in the wheat flour samples supplied by our patients. We found that 30% of the patients had IgE-mediated hypersensitivity of Ld. Of these, 23% did not have a relationship with any bakery or agriculture. We conclude that the prevalence of sensitization to Ld in patients sensitized to wheat flour is important.

Adolescent↗

Members of the alpha-amylase inhibitors family from wheat endosperm are major allergens associated with baker's asthma.

We have identified the major antigens or IgE binding components from wheat flour. Thirty-five sera from patients with baker's asthma were used to analyze the reaction with wheat salt-soluble proteins. We found a 15 kDa SDS-PAGE band which reacted with all sera tested. Purified members of the alpha-amylase inhibitor family, which are the main components of the 15 kDa band, were recognized by specific IgE when tested with a pool of reactive sera. Immunodetection after two-dimensional electrophoretic fractionation of crude inhibitor preparations from wheat endosperms also detected several inhibitor subunits as major low-molecular-weight allergens.

Allergens↗

Bakers' asthma: prevalence and evaluation of immunotherapy with a wheat flour extract.

One hundred thirty-nine bakers and pastry cooks were included in a prevalence study of IgE-mediated hypersensitivity to wheat flour demonstrated by skin tests, specific IgE to wheat flour (RAST), and inhalation challenge. From the sensitized workers, we selected 30 asthmatic patients. Twenty patients were treated with a standardized wheat flour extract, and ten with a placebo in a double-blind clinical trial. Before and after immunotherapy we performed tests in vivo (skin tests with wheat flour and methacholine tests), and in vitro (total IgE and specific IgE to wheat flour). We found substantial prevalence of wheat flour allergy (25.17% of workers), and a significant decrease (P less than .001) in hyperresponsiveness to methacholine, skin sensitivity (P = .002), and specific IgE (P less than .005) to wheat flour after 20 months of immunotherapy. There was also significant subjective improvement (P less than .001). The placebo group showed no changes in these variables.

Adolescent↗

Allergenic variability in olea pollen.

Marked in vitro allergenic potency variations were observed among six different olive pollen batches as determined by RAST inhibition, in direct correlation with the content of a multimeric component of 55,000 D as analyzed by size-exclusion high performance liquid chromotography. Electrophoretical patterns displayed differences in a heterogeneous band of 20,000 D and isoelectric point around 5, which probably represents the monomeric form of the major allergen.

Allergens↗

Exercise-induced anaphylactic reaction to grain flours.

On rare occasions, reproducible exercise-induced anaphylactic reactions (EIA) occur in some patients only after certain foods have been eaten before exercise, yet eating these foods alone or exercising alone causes no symptoms. This special response has been evident sometimes with shellfish, nuts, and wheat. We describe a patient in whom grain flour was a triggering factor for EIA. Skin tests and RAST were positive for grain flours. Normally, the patient tolerated grain flours without symptoms and IgE mechanisms had not been suspected. Testing for food hypersensitivity may be important in patients with EIA.

Anaphylaxis↗

New alpha-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare).

Barley CM-proteins are a group of at least five salt-soluble components (CMa-e) that can be selectively extracted from endosperm with chloroform/methanol mixtures. N-terminal sequences of proteins CMa, CMb and CMc have been determined and found to be homologous to those previously determined for CMd and CMe, an observation which confirms that their structural genes are members of a dispersed multi-gene family. The purified CM-proteins were tested against trypsin and against alpha-amylases from saliva, pancreas, Aspergillus oryzae, Tenebrio molitor and barley. Besides CMe, which was known to be a trypsin inhibitor, CMc also showed antitrypsin activity, whereas CMa was specifically active against the alpha-amylase from T. molitor and no inhibitory activity was found for proteins CMb and CMd. The evolutionary implications of these findings are discussed.

Amino Acid Sequence↗

Differential effects of high-lysine mutations on the accumulation of individual members of a group of proteins encoded by a disperse multigene family in the endosperm of barley (Hordeum vulgare L.).

The CM proteins are a group of major salt-soluble endosperm proteins encoded by a disperse multigene family. The effects of high-lysine mutations on the net accumulation in barley endosperm of three members of this group (CMa, CMb, and CMe) have been investigated. Genes CMa, CMb and CMe are located in chromosomes 1, 4, and 3 respectively. Protein CMe has been found to be identical with a previously described trypsin inhibitor. The three proteins have been quantified in the different genetic stocks by HPLC. The different high-lysine mutations have different effects on the expression patterns of the three genes: CMe is markedly decreased and CMa and CMb are increased in mutant Risø 1508, whereas all three proteins are decreased in Risø 527 and increased in Risø 7 with respect to the wild-type Bomi; CMa and CMb are increased and CMe is unaffected in mutant Risø 56 with respect to the wild-type Carlsberg II; and protein CMe is markedly decreased in Hiproly barley as compared with its sister line CI4362. The implications of these results in connection with the evolution of CM proteins and with the characterization of high-lysine mutations are discussed.

Amino Acid Sequence↗

The primary structure of the cytotoxin restrictocin.

The complete amino acid sequence of the single polypeptide chain of cytotoxin restrictocin has been determined. Its structure was established by automated Edman degradation of the intact molecule reduced and [14C]carboxymethylated and of fragments obtained by chemical cleavage of the protein with cyanogen bromide and BNPS-skatole and by enzymatic cleavage of the polypeptide chain with trypsin. The molecule consists of 149 amino acid residues with a calculated relative molecular mass of 16836. The protein presents two disulfide bridges, one between cysteine residues at positions 5 and 147 and the other one formed by cysteine residues at positions 75 and 131. The amino acid sequence of restrictocin shows a high degree of homology (86%) with that of the cytotoxin named alpha-sarcin.

Allergens↗

The optical properties of CuA in bovine cytochrome c oxidase determined by low-temperature magnetic-circular-dichroism spectroscopy.

The visible-near-i.r.-region m.c.d. (magnetic-circular-dichroism) spectrum recorded at low temperature in the range 450-900 nm is reported for oxidized resting mammalian cytochrome c oxidase. M.c.d. magnetization curves determined at different wavelengths reveal the presence of two paramagnetic species. Curves at 576, 613 and 640 nm fit well to those expected for an x,y-polarized haem transition with g values of 3.03, 2.21 and 1.45, i.e. cytochrome a3+. The m.c.d. features at 515, 785 and 817 nm magnetize as a S = 1/2 paramagnet with average g values close to 2, and simulated m.c.d. magnetization curves obtained by using the observed g values of CuA2+, i.e. 2.18, 2.03 and 1.99, fit well to the experimental observations. The form of the m.c.d. magnetization curve at 466 nm is curious, but it can be explained if CuA2+ and cytochrome a3+ contribute with oppositely signed bands at this wavelength. By comparing the m.c.d. spectrum of the enzyme with that of extracted haem a-bisimidazole complex it has been possible to deconvolute the m.c.d. spectrum of CuA2+, which shows transitions throughout the spectral region from 450 to 950 nm. The m.c.d.-spectral properties of CuA2+ were compared with those of a well-defined type I blue copper centre in azurin isolated from Pseudomonas aeruginosa. The absolute intensities of the m.c.d. signals at equal fields and temperatures for CuA2+ are 10-20-fold greater than those for azurin. The optical spectrum of CuA2+ strongly suggests an assignment as a d9 ion rather than Cu(I) bound to a thiyl radical.

Animals↗

Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics.

A procedure is described for the purification of cytochrome c peroxidase from Pseudomonas aeruginosa involving extraction by sonication, followed by acid precipitation and chromatography on only two types of gel. The final preparation had a purity ratio A407/A280 of 4.2, and was found to be essentially pure by isoelectric focusing. The enzyme was shown to be unstable during degassing under vacuum except in the presence of detergent. The kinetics of CO binding to dithionite-reduced peroxidase were studied with stopped-flow and flash-photolysis techniques, and the results obtained between pH 5 and 7 suggest the existence of two forms of dithionite-reduced enzyme in slow equilibrium.

Carbon Monoxide↗

Septic arthritis due to Arizona hinshawii.

Arizona hinshawii, a gram negative bacillus which bears antigenic similarities to genus Salmonella is an uncommon cause of human disease. We report 3 patients who in an immunocompromised state developed septic arthritis due to Arizona hinshawii. Treatment with systemic antibiotics and repeated joint aspiration was successful. The infection was recurrent in 2 patients and 1 died of septicemia. Previous cases of Arizona hinshawii septic arthritis are reviewed.

Adult↗