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ambrosia dumosa/carbohydrate

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ArtiklidKliinilistes uuringutesPatendid
11 tulemused

Uptake of carbohydrate by polyribosomes during the immune response to ragweed antigen.

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The N-glycans from soluble extracts of ten pollens were examined. The pyridylaminated oligosaccharides derived from these sources were subject to gel filtration and reverse-phase HPLC, in conjunction with exoglycosidase digests, and in some cases matrix-assisted laser desorption-ionisation mass

The amino acid sequence of ragweed pollen allergen Ra5.

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The complete amino acid sequence of Ra5, a ragweed pollen allergen, has been determined. Allergen Ra5 is a low molecular weight protein of 45 residues derived from Ambrosia elatior, the short ragweed. It contains no detectable carbohydrate or lipid and has four disulfide bridges. The total structure

Amino acid sequence of ragweed allergen Ra3.

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The complete amino acid sequence of ragweed pollen allergen Ra3 has been determined. The molecule consists of 101 amino acid residues and to date is the only allergen isolated from Ambrosia elatior (short ragweed) which contains carbohydrate. This particular preparation of allergen has a single,

Aqueous-organic solvent extraction of water-insoluble protein from ragweed pollen.

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A water-insoluble material was obtained from either short ragweed (Ambrosia elatior) or false ragweed (Franseria acanthicarpa) pollen extracted by organic solvent (50% N,N-dimethylformamide). Further investigation of this water-insoluble material showed it contained at least five proteins. Two of

Patterns of functional enzyme activity in fungus farming ambrosia beetles.

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BACKGROUND In wood-dwelling fungus-farming weevils, the so-called ambrosia beetles (Curculionidae: Scolytinae and Platypodinae), wood in the excavated tunnels is used as a medium for cultivating fungi by the combined action of digging larvae (which create more space for the fungi to grow) and of
A protein allergen, Ra5, was isolated by column chromatographic procedures from the aqueous extract of short ragweed pollen by Lapkoff and Goodfriend. The allergen was obtained in a highly homogenous form, was devoid of carbohydrate and had the low molecular weight of 5100 daltons. A report will be

Two variants of ragweed allergen Ra3.

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Two disc electrophoretic forms of Ra3 (I and II) were isolated by column chromatography in yields of 30 and 10 mg/kg pollen, respectively. On the basis of 8% carbohydrate content (determined for Ra3I and assumed for Ra3II), the major and minor forms had essentially identical molecular weights
During the first few years of elevated atmospheric [CO(2)] treatment at the Nevada Desert FACE Facility, photosynthetic downregulation was observed in desert shrubs grown under elevated [CO(2)], especially under relatively wet environmental conditions. Nonetheless, those plants maintained increased

Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A).

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Lung surfactant protein A (SP-A) is the most abundant surfactant-associated protein present in the lung. A receptor for SP-A has been shown to be present on A549 alveolar type II cells and on other cell types, including alveolar macrophage. The SP-A receptor on A549 cells has been identified as the

Characterization and discrimination of pollen by Raman microscopy.

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The chemical characterization and discrimination of allergy-relevant pollen (common ragweed (Ambrosia artemisiifolia), white birch (Betula pendula), English oak (Quercus robur), and European linden (Tilia cordata)) has been studied by Raman microscopy. Spectra were obtained at different excitation
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