poa/protease

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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

Expression and thrombin cleavage of Poa p IX recombinant allergens fused to glutathione S-transferase.

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The high-level expression and purification of Poa p IX recombinant grass pollen allergens were examined utilizing a modified pGEX plasmid, designated as pGEX 2T-1. This vector permits frame-1 ligation of lambda gt11 cDNA inserts and cleavage of the recombinant allergenic protein from the fusion

Small hydroxyethylene-based peptidomimetics inhibiting both HIV-1 and C. albicans aspartic proteases.

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We have extended a highly flexible method for rapidly assembling aspartic protease inhibitors to produce symmetric and asymmetric monohydroxyethylene peptidomimetics. This method is based on the prior synthesis of the central non-cleavable peptide-bond isostere [NH(2)-P(1)psiP1'-NH(2);

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

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

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

Effects of heavy metal pollution on enzyme activities in railway cut slope soils.

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Railway transportation is an important transportation mode. However, railway transportation causes heavy metal pollution in surrounding soils. Heavy metal pollution has a serious negative impact on the natural environment, including a decrease of enzyme activities in soil and degradation of

IgE-binding trypsin inhibitors in plant pollen extracts.

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In an attempt to access the possible role of protease-antiprotease mechanisms of non-immune defence in pollinosis, only low levels of trypsin-, kallikrein- or plasmin-like proteinases could be detected in aqueous pollen extracts. In contrast, several pollen species displayed appreciable trypsin

Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophilia strain.

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A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by

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

Collaboration between grass seedlings and rhizobacteria to scavenge organic nitrogen in soils.

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Plants require nitrogen (N) to make proteins, nucleic acids and other biological molecules. It is widely accepted that plants absorb inorganic forms of N to fill their needs. However, recently it has become clear that plants also have the capacity to absorb organic N from soils. In this paper we

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