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[Extracellular proteases of mycelial fungi as participants of pathogenic processes].
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The interest in proteases secreted by mycelial fungi is due to several reasons of which one of the most important is their involvement in the initiation and development of the pathogenic process. A comparison of saprophytic and phytopathogenic mycelial fungi revealed one characteristic feature,
Mass spectrometric analysis of electrophoretically separated allergens and proteases in grass pollen diffusates.
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BACKGROUND
Pollens are important triggers for allergic asthma and seasonal rhinitis, and proteases released by major allergenic pollens can injure airway epithelial cells in vitro. Disruption of mucosal epithelial integrity by proteases released by inhaled pollens could promote allergic
Oncostatin M synergises with house dust mite proteases to induce the production of PGE(2) from cultured lung epithelial cells.
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The release of PGE(2) and nitric oxide (NO) from the respiratory epithelium may act to dampen inflammation. In other tissues, oncostatin M (OSM), a potent inducer of epithelial antiproteases, has also been shown to interact with IL-1beta to stimulate PGE(2) release. However, whether OSM interacts
Studies on the specificity of human IgE-antibodies to the plant proteases papain and bromelain.
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The sera of seven patients clinically hypersensitive to papain--in one case also to baromelain--and the sera of sixty asthmatic patients with allergies to other inhalant and food allergens were investigated for IgE antibody activity to the plant proteases papain and bromelain and to common allergens
Effect of carbohydrase and protease on growth performance and gut health of young broilers fed diets containing rye, wheat, and feather meal.
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An experiment was conducted to characterize a gut health challenge model consisting of a diet containing rye, wheat, and feather meal and a mild mixed-species Eimeria challenge, and to evaluate the effect of carbohydrase and protease on growth performance and gut health of young broilers. The study
Characterization of proteases, proteins, and eicosanoid-like substances in soluble extracts from allergenic pollen grains.
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BACKGROUND
Pollen is an important trigger of seasonal rhinitis, conjunctivitis, and/or allergic asthma, and an exacerbating factor in atopic dermatitis. Pollen grains contain allergen proteins, enzymes, and bioactive lipid mediators, the latter two possibly involved in the pathogenesis of allergic
Plant Proteases: From Key Enzymes in Germination to Allies for Fighting Human Gluten-Related Disorders.
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Plant proteases play a crucial role in many different biological processes along the plant life cycle. One of the most determinant stages in which proteases are key protagonists is the plant germination through the hydrolysis and mobilization of other proteins accumulated in seeds and cereal grains.
A scaleable manufacturing process for pro-EP-B2, a cysteine protease from barley indicated for celiac sprue.
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Celiac Sprue is an inflammatory disease of the small intestine triggered by ingestion of dietary gluten, a family of glutamine and proline rich proteins found in common foodgrains such as wheat, rye, and barley. One potential therapy for this lifelong disease anticipates using an oral protease to
Protease inhibitors in various flours and breads: Effect of fermentation, baking and in vitro digestion on trypsin and chymotrypsin inhibitory activities.
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In this study trypsin (TIA) and chymotrypsin inhibitory (CIA) activities were determined in the extracts of wheat, rye mix, mixed cereals and, whole wheat flours and, breads made with these flours. In addition, effects of fermentation, baking and in vitro digestion on TIA and CIA were studied. Whole
Partial Purification and Characterization of a Phytochrome-degrading Neutral Protease from Etiolated Oat Shoots.
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A factor catalyzing the in vitro degradation of oat phytochrome in crude extracts has been shown to be a proteolytic enzyme. The enzyme, an endoprotease, has been purified about 600-fold from dark-grown oat shoots by chromatography on ion exchange and molecular seive gels. The pH-activity curve is
[Plant protease inhibitors. 3. Purification of trypsin inhibitors from germs of wheat and rye seed; localization of the active centers].
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Purification and characterization of a trypsin inhibitor from Plathymenia foliolosa seeds.
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A novel trypsin inhibitor (PFTI) was isolated from Plathymenia foliolosa (Benth.) seeds by gel filtration chromatography on a Sephadex G-100, DEAE-Sepharose, and trypsin-Sepharose columns. By SDSPAGE, PFTI yielded a single band with a M(r) of 19 kDa. PFTI inhibited bovine trypsin and bovine
Variation in the primary structure of waxy proteins (granule-bound starch synthase) in diploid cereals.
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The molecular weights of waxy proteins, by SDS-PAGE, and the N-terminal amino acid sequences of mature protein and of V8 protease-induced fragments were determined in diploid cereals. The homology of the primary structure was relatively high among cereals examined here, and there appeared to be a
Identification and characterization of wheat grain albumin/globulin allergens.
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Bakers' asthma, an immediate-type allergic response to the inhalation of cereal flours, is an important occupational disease among workers of the baking and milling industries, and the salt-soluble proteins of wheat and rye flour dust are considered the most relevant allergens. In order to identify
The dark reactions of rye phytochrome in vivo and in vitro.
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The dark reactions of Secale cereale L. cv. Balbo phytochrome have been investigated in coleoptile tips and in extensively purified extracts of large molecular weight phytochrome. Destruction, but not reversion, was detected in vivo. The effects of various inhibitors of an in vitro
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