lolium/protease

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Substrate preference profiles of proteases released by allergenic pollens.

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BACKGROUND Pollens are important triggers for allergic asthma and seasonal rhinitis. We have recently reported that proteases released by major allergenic pollens can injure airway epithelial cells in vitro. Disruption of epithelial integrity by proteases released following deposition of pollens on

A Novel Fungal Protease Expressed in Endophytic Infection of Poa Species.

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The fungus Acremonium typhinum produces a novel endoprotease during symbiotic endophytic infection of the grass, Poa ampla. This protease is unusual because it is highly active in the presence of sodium dodecyl sulfate. The enzyme is a thiol-containing serine protease and is localized to a crude

Characterisation of a cysteine protease cDNA from Lolium multiflorum leaves and its expression during senescence and cytokinin treatment.

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A cysteine protease cDNA clone (See1) highly homologous to barley aleurain was isolated from Lolium multiflorum leaves. During leaf senescence, expression of the See1 mRNA and protein was strongly enhanced. In dark-incubated leaf segments, cytokinin delayed senescence and reduced expression of both

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

Mutualistic fungal endophytes express a proteinase that is homologous to proteases suspected to be important in fungal pathogenicity.

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Many cultivated and wild grass species are hosts to mutualistic fungal endophytes. These associations are ecologically and agronomically significant, yet little is known regarding the physiological aspects of the interaction. In the Poa ampla/Acremonium typhinum interaction, a fungal serine

Dark-mediated dormancy release in stratified Lolium rigidum seeds is associated with higher activities of cell wall-modifying enzymes and an apparent increase in gibberellin sensitivity.

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Dormancy release in freshly matured, imbibed annual ryegrass (Lolium rigidum) seeds is inhibited by light and involves a decrease in seed sensitivity to abscisic acid. Other processes involved in dormancy release in the dark were investigated by measuring seed storage compound mobilisation and the

Enzymes of nitrogen mobilization in detached leaves of Lolium temulentum during senescence.

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During the senescence of Lolium temulentum leaf sections in the dark, asparagine and glutamine accumulated as the level of soluble protein declined. During the first 3-4 days after detachment, when the rate of protein loss was maximal, a four-fold increase in acid protease activity (EC 3.4.4.?)

MALDI-TOF MS analysis of labile Lolium perenne major allergens in mixes.

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BACKGROUND It is well known that allergen extracts used for specific therapy of allergic disorders are commonly stored as mixtures, causing an alteration of its stability. OBJECTIVE The aim of this report is to identify pollen allergens susceptible to degradation during storage of mixtures

Organic residues as immobilizing agents in aided phytostabilization: (II) effects on soil biochemical and ecotoxicological characteristics.

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Sewage sludge (SS), municipal solid waste compost, and garden waste compost (GWC) were used as immobilizing agents in aided phytostabilization of an acid metal-contaminated soil affected by mining activities. The organic residues were applied at 25, 50 and 100 Mg ha(-1) (dry weight basis) and

Effects of interaction between pollen coat eluates and pistil at the molecular level in self-compatible and self-incompatible plants of Lolium multiflorum Lam.

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Two-dimensional electrophoresis (2-DE) of soluble proteins and enzymes was performed and specific activities of 5 enzymes (esterase, pectinesterase, acid phosphatase, protease and diaphorase) were determined in stigmas of Lolium multiflorum (Italian ryegrass) treated with self or foreign pollen coat

Lol p XI, a new major grass pollen allergen, is a member of a family of soybean trypsin inhibitor-related proteins.

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BACKGROUND Monoclonal antibodies were obtained against an unknown allergen from Lolium perenne grass pollen. The allergen had an apparent molecular mass of 18 kd on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Earlier immunoblotting studies had shown that carbohydrate-specific IgG

An assessment of the ability of the stay-green phenotype in lolium species to provide an improved protein supply for ruminants.

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The stay-green phenotype results from a naturally occurring mutation in which senescent leaves retain their chlorophyll and the associated apoprotein, LHCPII. Protection of this protein pool could deliver grass with enhanced protein content and could decrease the extent of protein degradation by

Comparative proteomic analyses reveal the proteome response to short-term drought in Italian ryegrass (Lolium multiflorum).

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Drought is a major abiotic stress that impairs growth and productivity of Italian ryegrass. Comparative analysis of drought responsive proteins will provide insight into molecular mechanism in Lolium multiflorum drought tolerance. Using the iTRAQ-based approach, proteomic changes in tolerant and

Injury to murine airway epithelial cells by pollen enzymes.

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BACKGROUND Pollens are important triggers for asthma but the mechanism of sensitisation to their proteins remains poorly understood. The intrinsic protease activity of some allergens may contribute to sensitisation by disrupting the integrity of the airway epithelial barrier. Pollens release a

Modification of senescence in ryegrass transformed with IPT under the control of a monocot senescence-enhanced promoter.

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We report here the genetic modification of ryegrass senescence. Embryogenic cell suspensions of Lolium multiflorum were transformed by microprojectile bombardment with plasmid constructs containing 1.98 kb of the 5' flanking sequence of SEE1 (a maize cysteine protease gene showing enhanced

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