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PubMed1967

The subcellular distribution and biosynthesis of castaprenols and plastoquinone in the leaves of Aesculus hippocastanum.

Intact chloroplasts and cell walls were prepared from horse-chestnut leaves that had previously metabolized [2-(14)C]mevalonate. The bulk of the castaprenols and plastoquinone-9 was found within the chloroplasts. The remaining portion of the castaprenols was associated with the cell-wall preparation whereas that of the plastoquinone-9 was probably localized in the soluble fraction of the plant cell. The (14)C content of these compounds of different cell fractions indicated the presence of polyisoprenoid-synthesizing activity both inside and outside the chloroplasts. This was confirmed by the relative incorporation of (14)C when ultrasonically treated and intact chloroplasts were incubated with [2-(14)C]mevalonate. As the leaves aged (on the tree) an increase in extraplastidic castaprenols and plastoquinone-9, together with associated synthesizing activities, was observed.

Alcohols↗
PubMed1992

Horse chestnut (Aesculus hippocastanum) pollen: a frequent cause of allergic sensitization in urban children.

We investigated the incidence of allergic sensitization and the risk factors underlying sensitization in 214 urban children exposed to horse chestnut pollen. By means of the Phadezym RAST, we found IgE specific to horse chestnut pollen in 12.6% of the urban children, whereas it occurred in only 1.9% of control subjects recruited from a rural area. Reports of allergic symptoms in spring during the horse chestnut pollen load coincided with the presence of specific IgE in 5.1% of the urban group as against 1.4% of the recruited from the rural area. Environmental factors other than those related to urban living and higher horse chestnut pollen counts had no significant impact on allergic sensitization. Increased total IgE levels (greater than 100 kU/l), however, and the sensitization to pollen of other species significantly raised the odds for sensitization to chestnut pollen. They were highest in highly atopic children with sensitization to pollen, especially to that of plane trees (OR = 73.9). These results suggest the relevance of horse chestnut pollen because of the high allergic sensitization rate among urban children, and they should also be borne in mind when it comes to the planting of trees in urban areas.

Allergens↗
PubMed1992

Neurodepressive action of a piscicidal glycoside of plant, Aesculus indica (Colebr.) in fish.

Sublethal concentration (2.6 mg/l) of a triterpene based piscicidal glycoside of A. indica damaged the neurons, fibre tracts and central correlation sites for gustatory, tactile and visceral sensory impulses in medulla oblongata of fish after prolonged poisoning. The fear, sinking to bottom, lack of schooling and non discriminatory pattern in treated fish were because of neurodepression. The jerky movement, ventilatory inefficiency, swallowing air bubbles and light pinkness of gills were due to the degradation of respiratory centres in the vagal lobes of toxified fish.

Animals↗
PubMedDate not supplied

[Isolation of lectin from horse chestnut (Aesculus hippocastanum L.) seeds and study of its interaction with carbohydrates and glycoproteins].

The lectin from horse chestnut seeds was obtained by affinity chromatography on a sorbent prepared from the egg white, 95 mg of lectin per 1 kg of fresh seeds being obtained. Molecular weight was determined by gel-filtration on tojopearl HW-55 and it composed 132 kDa. SDS-polyacrylamide gel electrophoresis revealed the presence of one component with molecular weight of 33 kDa. One band has been revealed by means of disc-electrophoresis in acidic (pH 4.5) and alkaline system (pH 8.9). Sugar was not detected in the lectin. Amino acid composition of the lectin has been determined. The lectin agglutinated horse erythrocytes in minimal concentration of 9.5 ngml, to the less extent rabbit (4.9 mkg/ml), rat (62 mkg/ml), human (73 mkg/ml), but did not agglutinate erythrocytes of a sheep and cow. Purified lectin did not interact with monosaccharides, but interacted with O-glycans.

Amino Acids↗